Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.89881046
This Mr 141000 calmodulin binding protein is identified as caldesmon on the basis of Ca2+ dependent interaction with calmodulin , subunit Mr , Ca2+ independent interaction with skeletal muscle F actin , Ca2+ dependent competition between calmodulin and F actin for caldesmon , and tissue content . . 0.89881046^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.56367592
Reversal of caldesmon binding to myosin with calcium calmodulin or by phosphorylating caldesmon . 0.56367592^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.72145658
Thus although both N and C terminal domains of calmodulin are involved in the interaction with caldesmon and calponin , the C terminal part of calmodulin ( residues 78 148 ) is of special importance and has the highest contribution for caldesmon and calponin binding . . 0.72145658^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.65096197
Comparison of this fragment with others suggests that a small region of caldesmon is responsible for at least part of the interaction with both calmodulin and actin . . 0.65096197^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.78835491
Binary complex interactions between caldesmon and tropomyosin , and calmodulin and tropomyosin , and ternary complex interaction involving the three proteins were studied using viscosity , electron microscopy , fluorescence and affinity chromatography techniques . 0.78835491^^^ The result is consistent with a model that in the absence of Ca2+ , calmodulin binds weakly to either caldesmon or tropomyosin and has little effect on the tropomyosin caldesmon interaction ; whereas , Ca 2 ( + ) calmodulin interacts with caldesmon and reduces its affinity to tropomyosin . . 0.59670633^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.9750756
Ca2+ regulation in this system does not depend on a simple competition between Ca2+ calmodulin and actin for binding to caldesmon . 0.9750756^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.79404711
Caldesmon was found to bind to calmodulin in the presence of Ca2+ , with an affinity of 10 ( 6 ) M 1 . 0.79404711^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.98229187
This effect may be due to the direct interaction of caldesmon with a Ca2+ binding protein such as calmodulin or phosphorylation of caldesmon by a Ca2+ dependent kinase . 1 have found that Ca2+ switches on aorta thin filaments in less than 10 s , whereas the caldesmon in the thin filaments is phosphorylated only slowly ( half time greater than 10 min ) and the maximum phosphorylation is very low ( 1 molecule per 7 molecules of caldesmon ) . 1 conclude that the phosphorylation of caldesmon hypothesis is untenable . . 0.98229187^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.63446695
As indicated by a decrease in maximum tryptophan fluorescence emission of caldesmon ( about 14 % at 1 : 1 molar ratio ) and displacement of calmodulin from its complex with caldesmon , chicken gizzard calcyclin binds caldesmon . 0.63446695^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.67406579
Calmodulin has been shown to interact with the COOH terminal domain of gizzard h caldesmon at three sites , A ( residues 658 666 ) , B ( residues 687 695 ) , and B ' ( residues 717 725 ) , each of which contains a Trp residue [ Zhan et al . ( 1991 ) J . 0.67406579^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.57219043
Calmodulin binds to caldesmon in an antiparallel manner . 0.57219043^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.5996091
It reverses caldesmon inhibition at pCa 5 under conditions where CaM is largely inactive , it binds to caldesmon when complexed with actin and tropomyosin rather than displacing it and it binds to caldesmon independently of [ Ca2+ ] . 0.5996091^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.58298522
Replacement of Lys 75 of calmodulin affects its interaction with smooth muscle caldesmon . 0.58298522^^^ The interaction of smooth muscle caldesmon with synthetic calmodulin ( SynCam ) and its five mutants with replacement of Lys 75 was analyzed by means of intrinsic Trp fluorescence , zero length crosslinking and by caldesmon induced inhibition of actomyosin ATPase activity . 0.53362799^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In the presence of Ca2+ , calmodulin competed with phospholipids for the interaction with the caldesmon peptides . ^^^ The C terminal part of caldesmon contains three peptides with a primary structure similar to that of the calmodulin and phospholipid binding site of neuromodulin . ^^^ These sites may be involved in the interaction of caldesmon with calmodulin and phospholipids . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Phosphorylation of caldesmon attenuated slightly its interaction with actin and had no effect on its binding to calmodulin and tropomyosin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
GS17C , a peptide that contains the residues from Gly 651 to Ser 667 of the caldesmon sequence plus an added cysteine at the C terminus , binds calmodulin in a Ca ( 2+ ) dependent manner and also binds to F actin but does not inhibit actomyosin ATPase activity ( Zhan , Q . , Wong , S . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Interaction of calmodulin with phospholamban and caldesmon : comparative studies by 1H NMR spectroscopy . ^^^ In order to identify comparative aspects of the interaction of calmodulin with its target proteins , proton magnetic resonance studies of complex formation between calmodulin and defined segments of phospholamban and caldesmon have been undertaken . ^^^ We contrast here a calmodulin binding segment in the C terminal region of caldesmon localised by 1H NMR study of the interface ( s ) between the two proteins . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Like calmodulin , caltropin could release the inhibitory effect of caldesmon in the presence of Ca2+ . ^^^ Caltropin was at least as potent as calmodulin , if not better , in reversing the inhibitory effect of caldesmon in the presence of calcium , making it a potential Ca2+ factor in regulating caldesmon in smooth muscle . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The binding of caldesmon to microtubules was inhibited in the presence of Ca2+ and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Unlike calmodulin , addition of caldesmon , actin or bovine serum albumin did not increase the release . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We have found that both in vivo and in vitro phosphorylation of caldesmon causes similar changes in the properties , including reduction in actin , calmodulin , and myosin binding of caldesmon , and a decrease in the inhibition of actomyosin ATPase by caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The binding of caldesmon to microtubules was inhibited in the presence of Ca2+ and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Of the CaMBP expressed , phosphodiesterase , calcineurin , caldesmon , and adducin cross linked with CaM DAP in the loaded SK N SH cells . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In addition , these cells have the potential for regulation at the thin filament level by caldesmon and calponin , both of which bind calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
It has been recently discovered that nonmuscle caldesmon , an actin and calmodulin binding microfilament associated protein of relative molecular mass Mr = 83 , 000 , is dissociated from microfilaments during mitosis , apparently as a consequence of mitosis specific phosphorylation . cdc 2 kinase , which is a catalytic subunit of MPF ( maturation or mitosis promoting factor ) , is found to be responsible for the mitosis specific phosphorylation of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Three such mechanisms have emerged : ( 1 ) the actin , tropomyosin , and calmodulin binding protein , calponin ; ( 2 ) the actin , myosin , tropomyosin , and calmodulin binding protein , caldesmon ; and ( 3 ) the Ca ( 2+ ) and phospholipid dependent protein kinase ( protein kinase C ) . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Using a series of truncated caldesmons expressed in Escherichia coli , the common calmodulin , tropomyosin , and actin binding sites and the minimum regulatory domains , which are involved in the Ca 2 ( + ) dependent regulation of actin myosin interaction , have been identified within the limited consensus sequences ( residues 381 433 for l caldesmon and residues 636 688 for h caldesmon ) . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
This dependence on conditions is also characteristic of the calmodulin caldesmon interaction . 3 . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Since myosin also binds to actin in the vicinity of Cys 374 and since caldesmon inhibits actomyosin ATPase activity by the reduction of myosin binding to actin , then the inhibition might be by caldesmon sterically hindering or blocking myosin ' s interaction with actin . [ Ca2+ ] Calmodulin , which reverses the inhibition of the ATPase activity , decreases the yield of the cross linked species , suggesting a weakening of the caldesmon actin interaction in the cross linked region . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon inhibited actomyosin with a 10 fold greater potency than calponin in the presence of tropomyosin and inhibition could be reversed by Ca2+ calmodulin under certain conditions . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Specific identification and subcellular localization of three calmodulin binding proteins in the rat gonadotrope : spectrin , caldesmon , and calcineurin . ^^^ In the present study , we have used a calmodulin overlayer assay combined with Western blotting to determine the molecular identity of three calmodulin binding proteins in rat gonadotropes : the alpha subunit of spectrin ( Mr greater than 205 , 000 ) , caldesmon ( Mr 84 , 000 ) , and the alpha subunit of calcineurin ( Mr 60 , 000 ) . ^^^ Like caldesmon from other sources , the Mr 84 , 000 component remains soluble after heat treatment and preferentially binds either filamentous actin or calmodulin , depending on the Ca2+ concentration . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The interaction of the 34 kDa fragment of caldesmon ( like that of the intact molecule ) with calmodulin is accompanied by a blue shift of the fluorescence emission maximum and an increase in the relative quantum yield . ^^^ Computer calculated binding constants show that the binding of calmodulin to the 34 kDa fragment ( K = 2 . 5 10 10 ( 5 ) M 1 ) is of two orders of magnitude weaker than that to intact caldesmon ( K = 1 . 4 10 10 ( 7 ) M 1 ) . ^^^ Binding of calmodulin to caldesmon and to the 34 kDa fragment affects their interaction with tropomyosin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Mechanism for the inhibition of acto heavy meromyosin ATPase by the actin / calmodulin binding domain of caldesmon . ^^^ Caldesmon , an actin / calmodulin binding protein , inhibits acto heavy meromyosin ( HMM ) ATPase , while it increases the binding of HMM to actin , presumably mediated through an interaction between the myosin subfragment 2 region of HMM and caldesmon , which is bound to actin . ^^^ In order to study the mechanism for the inhibition of acto HM ATPase , we utilized the chymotryptic fragment of caldesmon ( 38 kDa fragment ) , which possesses the actin / calmodulin binding region but lacks the myosin binding portion . ^^^ The 38 kDa fragment induced inhibition is partially reversed by calmodulin at a 10 : 1 molar ratio to caldesmon fragment ; the reversal was more remarkable in 100 mM ionic strength at 37 degrees C than in 20 or 50 mM at 25 degrees C . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon : a bifunctional ( calmodulin and actin ) binding protein which regulates stimulated gonadotropin release . ^^^ Recently we have specifically identified three CaM binding proteins of the gonadotrope as calcineurin , caldesmon , and spectrin . ^^^ Caldesmon ( identified by seven polyclonal and a monoclonal antibody , as well as by functional characteristics ) appears to be a CaM regulated , F actin binding , protein . ^^^ This finding , along with the previous observations that GnRH provokes a sufficient rise in intracellular Ca2+ to allow CaM to redistribute and bind proteins which it regulates , suggests a role for caldesmon in GnRH stimulated gonadotropin release from the pituitary . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Turkey gizzard caldesmon : complete sequence of a C terminal thrombic fragment that binds actin , tropomyosin and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
This inhibitory effect of caldesmon was relieved upon addition of excess calmodulin and Ca2+ . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Chem . 266 , 6678 6681 ) can be phosphorylated in vitro by p34cdc2 kinase resulting in the inhibition of caldesmon binding to F actin and Ca ( 2+ ) calmodulin . ^^^ Phosphorylation of Ser667 / Thr673 and Thr696 / Ser702 account for about 90 % of the total level of phosphorylation and these sites are located within the 10 kDa CNBr fragment at the COOH terminal end of caldesmon known to bind actin and Ca ( 2+ ) calmodulin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
A calmodulin binding peptide of caldesmon . ^^^ We found that GS17C indeed binds calmodulin in a Ca ( 2+ ) dependent manner ( Kd = 8 10 10 ( 7 ) M ) and appears to compete with caldesmon . ^^^ Interestingly , this synthetic peptide also co sediments with F actin , binding to actin being displaceable by calmodulin , as in the case of the native caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Non muscle caldesmon , an 83K actin and calmodulin binding protein , is dissociated from microfilaments during mitosis , apparently as a consequence of mitosis specific phosphorylation . ^^^ We now report that cdc 2 kinase phosphorylates caldesmon in vitro principally at the same sites as those phosphorylated in vivo during mitosis , and that phosphorylation reduces the binding affinity of caldesmon for both actin and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The C terminal peptide of caldesmon interacts with calmodulin with an affinity one order of magnitude higher than that of native caldesmon . ^^^ Phosphorylation does not affect the interaction of caldesmon with calmodulin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
This was also corroborated by the continued ability of the modified caldesmon to bind to actin and calmodulin , and by the property of the 90 kDa proteolytic N terminal fragment to give an internally cross linked species of 60 kDa . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Carbethoxylation of a 1 : 1 molar complex of caldesmon and calmodulin in the presence of Ca2+ resulted in the stoichiometric N carbethoxylation of His 610 of caldesmon and His 107 of calmodulin . ^^^ Carbethoxy caldesmon , like the unmodified protein , bound to immobilized calmodulin ( in the presence of Ca2+ ) and to immobilized tropomyosin ( at low ionic strength ) . ^^^ We conclude that the predicted basic amphiphilic alpha helical sequence ( Arg 593 His 610 ) does not represent the calmodulin binding site of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
F actin or calmodulin in the presence of Ca2+ blocks the phosphorylation of caldesmon . ^^^ The phosphorylation sites were located in a 10 , 000 Da CnBr fragment at the COOH terminal end of the caldesmon molecule known to house the binding sites for actin and calmodulin ( Bartegi A . , Fattoum , A . , Derancourt , J . , and Kassab , R . ( 1990 ) J . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Localization of the calmodulin and the actin binding sites of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin . ^^^ The identity of caldesmon was confirmed by comparing the images of caldesmon alone with those of the caldesmon calmodulin complex . ^^^ In the samples of caldesmon crosslinked with calmodulin , we noticed the existence of complexes containing two calmodulin molecules per caldesmon molecule , separated by a distance of 60 nm , consistent with the suggestion that each end of caldesmon can interact with calmodulin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Phosphorylation of high Mr caldesmon and its C terminal 35 kDa fragment reduced their binding abilities to both F actin and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Ca2+ / S100 protein , like Ca2+ / calmodulin , inhibited the binding of caldesmon to F actin in a concentration dependent manner and the inhibition was not observed in the absence of Ca2+ . ^^^ The molar ratio of S 100 protein to caldesmon required for half maximal restoration was about 0 . 3 , a value less than that in the case of calmodulin . ^^^ Taken together , our results suggest that a Ca 2 ( + ) binding protein other than calmodulin may regulate caldesmon dependent cellular functions . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The complementary segment of caldesmon has been localised to a 15 kDa thrombic fragment ( residues 483 578 ) derived from the N terminal portion of a 35 kDa proteolytic cleavage product from the C terminal of caldesmon whose interaction with actin is modulated by calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We found that non muscle caldesmon , a protein with a relative molecular mass ( Mr ) of 83 , 000 ( 83K ) which binds to actin and calmodulin , is dissociated from microfilaments during mitosis , apparently as a consequence of phosphorylation . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In support of this idea , our recent efforts to map the smaller non muscle form of caldesmon indicate that it retains the myosin and the calmodulin approximately actin binding domains , but is missing the central repeated region , arguing this region may serve to space the N and C terminal binding domains in smooth muscle . ^^^ Work from several laboratories has demonstrated that smooth muscle caldesmon is an elongated molecule with a calmodulin , tropomyosin , and actin binding region at the C terminus and a myosin binding domain at the N terminus . ^^^ Sequence determination has shown that smooth muscle caldesmon is smaller than previously believed , has demonstrated similarities between caldesmon and troponin T , and has suggested possible calmodulin binding peptides . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Native and wild type expressed caldesmon were indistinguishable in assays for inhibition of actin tropomyosin activation of myosin ATPase , reversal of inhibition by Ca 2 ( + ) calmodulin and binding to actin , actin tropomyosin , Ca 2 ( + ) calmodulin , tropomyosin and myosin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Interacting with caldesmon , calmodulin is shown to dissociate the caldesmon azolectin complex . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The effect of calmodulin on the incorporation of caldesmon has been examined by coinjection of caldesmon with calmodulin . ^^^ We have found that calmodulin retards the incorporation of caldesmon into stress fibers for a short period ( 10 min ) but not for a longer incubation ( 30 min ) . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Kinase activity associated with caldesmon is Ca2+ / calmodulin dependent kinase 2 . ^^^ The relationship of the kinase which co purifies with caldesmon to Ca2+ / calmodulin dependent protein kinase 2 ( CaM kinase 2 ) was investigated by studying the phosphorylation of bovine brain synapsin 1 , as well characterized substrate of CaM kinase 2 . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The substrate specificity of caldesmon kinase was similar to the rat brain calmodulin dependent multifunctional protein kinase 2 ( CaM PK 2 ) and phosphorylated brain synapsin and smooth muscle 20 kDa myosin light chain . ^^^ The observed properties were similar to brain CaM PK 2 , and , therefore , it was concluded that smooth muscle caldesmon kinase is the isozyme of CaM PK 2 in smooth muscle . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Calmodulin binding proteins in the nuclei of quiescent and proliferatively activated rat liver cells . alpha Spectrin , myosin light chain kinase ( MLCK ) , and caldesmon have been detected in the nuclei of rat liver cells by 125I calmodulin overlay , immunoblotting , and immunocytochemical methods . alpha Spectrin is localized in the nuclear matrix , nuclear envelope , and nuclear pores . ^^^ A 62 kDa protein ( p 62 ) which binds to calmodulin columns and shows immunological similarities to caldesmon is specifically located in the region surrounding the nuclear envelope and is associated with the heterochromatin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Location of the calmodulin and actin binding domains at the C terminus of caldesmon . ^^^ Digestion of caldesmon with carboxypeptidase Y is accompanied by loss of its ability to inhibit actomyosin ATPase activity and to bind actin and calmodulin . ^^^ Similarly , carboxypeptidase Y digestion of a terminal 40 kDa chymotryptic fragment of caldesmon abolishes its inhibition of the actomyosin ATPase and binding to actin and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Collectively , these results provide evidence that the effects of endothelin 1 on force generation and maintenance in vascular muscle may be dependent upon myosin light chain phosphorylation by Ca2+ calmodulin requiring myosin light chain kinase and upon a thin filament mechanism that is modulated by phosphorylation of caldesmon . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Although this molecular weight is similar to that of caldesmon , a known ubiquitous calmodulin binding protein , the protein did not react with caldesmon specific antibodies , nor did it display a proteolytic fragmentation pattern similar to that of the former . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The regulatory system of smooth muscle thin filaments is thought to involve a major calcium calmodulin and actin binding protein : caldesmon . ^^^ This work brings additional information to previous reports using an actin and calmodulin binding 25 kDa C terminal fragment of the caldesmon molecule [ ( 1989 ) J . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Characterization of the carboxyl terminal 10 kDa cyanogen bromide fragment of caldesmon as an actin calmodulin binding region . ^^^ A pair of 10 kDa peptides , designated CB a and CB b , was isolated by calmodulin Sepharose chromatography from a total CNBr digest of turkey gizzard caldesmon . ^^^ The CB a / CB b fragments inhibited , in a tropomyosin sensitive and Ca 2 ( + ) calmodulin dependent manner , the skeletal actomyosin subfragment 1 ATPase activity to a level close but not identical to that observed for the parent caldesmon . ^^^ Ca 2 ( + ) calmodulin was selectively cross linked to either caldesmon or the CNBr peptides with 1 ethyl 3 ( 3 dimethylaminopropyl ) carbodiimide producing 1 : 1 covalent complexes that were retained neither by phenyl Sepharose nor by immobilized calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Limited proteolysis , affinity chromatography , and immunoblotting have been used to define the domains of chicken gizzard caldesmon , caldesmon 120 , that interact with calmodulin , F actin , and a monoclonal antibody prepared using human platelet caldesmon . ^^^ The results suggest that interacting calmodulin and F actin binding sites are localized on a 38 kDa C terminal fragment of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In the presence of Ca2+ calmodulin , troponin C and S 100 protein form a complex with caldesmon . ^^^ Both S 100 protein and calmodulin effectively inhibit phosphorylation of caldesmon by Ca phospholipid dependent protein kinase . ^^^ At low ionic strength S 100 protein reverses the inhibitory action of caldesmon on the skeletal muscle acto heavy meromyosin ATPase more effectively than calmodulin . ^^^ It is supposed that in certain tissues and cell compartments the proteins belonging to the S 100 family are able to substitute for calmodulin in the caldesmon dependent regulation of actin and myosin interaction . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The 38 kDa chymotryptic fragment of caldesmon , which possesses the actin / calmodulin binding domain , was purified and utilized to study the mechanism for the inhibition of acto myosin ATPase by caldesmon . ^^^ The calmodulin restored the caldesmon induced binding of HMM to tropomyosin actin , but it had only a slight effect on the acto HMM ATPase . ^^^ These data suggest that the cooperative turning on of the smooth muscle tropomyosin actin by rigor bonds is modulated by the interaction of caldesmon , tropomyosin , and calmodulin on the thin filament . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The rate of degradation of calponin , unlike caldesmon and myosin light chain kinase , was accelerated when bound to calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Calmodulin decreases the potentiation effects of caldesmon as calmodulin inhibits actin binding of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Titration of kinase activity with calmodulin yielded maximum activity at substoichiometric ratios of calmodulin / caldesmon . ^^^ The sites of phosphorylation on caldesmon for calcium / calmodulin dependent protein kinase 2 and endogenous kinase were the same , but distinct from protein kinase C sites . ^^^ These results suggest that caldesmon is not a protein kinase and that kinase activity in caldesmon preparations is due to calcium / calmodulin dependent protein kinase II . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Turkey gizzard caldesmon : molecular weight determination and calmodulin binding studies . ^^^ Binding measurements , based on perturbation of the intrinsic tryptophan fluorescence of caldesmon in the presence of calmodulin , show that the interaction between the two proteins is strongly ionic strength and temperature dependent . ^^^ Fluorescence emission spectra and fluorescence anisotropy excitation spectra indicate that the tryptophanyl residues of caldesmon are located in solvent accessible regions of the molecule , where they exhibit a high degree of mobility even when calmodulin is bound . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Amino acid sequence studies on cyanogen bromide peptides of chicken caldesmon which bind to calmodulin . ^^^ Three major calmodulin binding cyanogen bromide peptides ( fragments A , B , and D ) were isolated from chicken gizzard muscle caldesmon and their amino acid sequences were determined . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Tropomyosin does not affect , while calmodulin strongly inhibits the phosphorylation of caldesmon by Ca phospholipid dependent protein kinase . ^^^ Data from one dimensional peptide mapping suggest that the sites phosphorylated by the enzyme are located in fragments with apparent molecular weights of 43 and 35 kDa , which are supposed to be located in the vicinity of N or C termini of the protein molecule and involved in the caldesmon interaction with actin and calmodulin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon structure and function : sequence analysis of a 35 kilodalton actin and calmodulin binding fragment from the C terminus of the turkey gizzard protein . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon has two calmodulin binding domains . ^^^ Chicken gizzard caldesmon was cleaved with chymotrypsin or CNBr , and the calmodulin binding fragments were isolated using an affinity column . ^^^ A comparison of the N terminal sequences of CB 40 and CT 40 with the complete sequence of caldesmon shows that the two calmodulin binding fragments in fact originate from different parts of the parent molecule . ^^^ Thus there exist two calmodulin binding sites in caldesmon , one in the N terminal half and the other in the C terminal half of the molecule . ^^^ This is consistent with the recent finding that up to two calmodulin molecules can be crosslinked to each caldesmon molecule ( Wang , C . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon is a smooth muscle and nonmuscle regulatory protein that interacts with actin , myosin , tropomyosin , and calmodulin . ^^^ Comparison with peptide sequences from a chymotryptic fragment that binds actin and calmodulin places this domain on the C terminus of caldesmon adjacent to the troponin T similarity . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
A recombinant protein produced in E . coli possesses calmodulin , F actin and tropomyosin binding abilities in common with the native h caldesmon . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon is a major calmodulin and actin binding protein of smooth muscle which interacts with calmodulin in a Ca2+ dependent manner or with actin in a Ca2+ independent manner . ^^^ Caldesmon can be phosphorylated in vitro by a co purifying Ca2+ / calmodulin dependent protein kinase and dephosphorylated by a protein phosphatase , both of which are present in smooth muscle . ^^^ Caldesmon containing endogenous kinase activity was rapidly phosphorylated ( to approx . 1 mol of Pi / mol of caldesmon in 5 min ) when reconstituted with actin , myosin , tropomyosin , calmodulin and myosin light chain kinase in the presence of Ca2+ and MgATP 2 . ^^^ All the bound phosphorylated caldesmon could be released by Ca2+ / calmodulin , with half maximal release at 0 . 11 microM Ca2+ , whereas only 62 % of the bound unphosphorylated caldesmon could be removed , with half maximal release at 0 . 16 microM Ca2+ . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon is universally associated with smooth muscle thin filaments , and reportedly interacts with actin , calmodulin , tropomyosin , and myosin . 1 attempted to determine the positions of the chymotryptic fragments which have been used to study the sites of such interactions in its primary structure . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Both these effects are reversed by calmodulin at a high molar excess over caldesmon in the presence of Ca2+ . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , a major actin and calmodulin binding protein , has been identified in diverse bovine tissues , including smooth and striated muscles and various nonmuscle tissues , by denaturing polyacrylamide gel electrophoresis of tissue homogenates and immunoblotting using rabbit anti chicken gizzard caldesmon . ^^^ Caldesmon was purified from vascular smooth muscle ( bovine aorta ) by heat treatment of a tissue homogenate , ion exchange chromatography , and affinity chromatography on a column of immobilized calmodulin . ^^^ The isolated protein shared many properties in common with chicken gizzard caldesmon : immunological cross reactivity , Ca2+ dependent interaction with calmodulin , Ca2+ independent interaction with F actin , competition between actin and calmodulin for caldesmon binding only in the presence of Ca2+ , and inhibition of the actin activated Mg2+ ATPase activity of smooth muscle myosin without affecting the phosphorylation state of myosin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Neither F actin nor calmodulin binding induces dramatic changes in susceptibility to chymotryptic cleavage and the sites of cleavage of caldesmon . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , an actin binding protein which also binds to calmodulin in the presence of Ca2+ , has been shown to be present in thin filaments isolated from smooth muscle . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , a calmodulin and actin binding protein , has been shown to exist in platelet . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We have examined the effects on the activities of three calmodulin dependent enzymes ( cAMP phosphodiesterase , caldesmon kinase and myosin light chain kinase ) of the dihydropyridine Ca2+ channel blocker felodipine and three analogues ( p chloro , oxidized and t butyl ) exhibiting different pharmacological potencies . ^^^ Felodipine and the p chloro analogue inhibited Ca2+ / calmodulin dependent caldesmon kinase with similar potencies ( IC 50 = 17 . 4 microM ) , whereas the oxidized and t butyl analogues caused no inhibition . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , an actin and calmodulin binding protein of smooth muscle , is a protein serine / threonine kinase capable of Ca2+ / calmodulin dependent autophosphorylation [ Scott Woo & Walsh ( 1988 ) Biochem . ^^^ Autophosphorylation does not affect the rate of hydrolysis of caldesmon ( free or bound to calmodulin ) by alpha chymotrypsin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon inhibition was not Ca2+ dependent , but inhibition could be reversed by further addition of Ca2+ and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The calmodulin and F actin binding sites of smooth muscle caldesmon lie in the carboxyl terminal domain whereas the molecular weight heterogeneity lies in the middle of the molecule . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Calmodulin in the presence of Ca2+ dissociates these bundles and restrains the inhibition of actomyosin ATPase , provided that it is used at a high molar excess over caldesmon . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , an actin and calmodulin binding protein , at caldesmon : actin molar ratio of 1 : 18 , binds equally to pure actin and actin containing stoichiometric amounts of bound tropomyosin . ^^^ The inhibition of activity by the caldesmon is reversed by the addition of calmodulin ( caldesmon : calmodulin molar ratio , 1 : 8 ) in the presence of Ca2+ . ^^^ The amount of caldesmon bound to actin in the presence of calcium calmodulin is 50 % more when actin filaments contain tropomyosin , indicating that the release of inhibition of the activity inhibited by caldesmon does not require complete release of caldesmon from actin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The effect of caldesmon is abolished by calmodulin in the presence of Ca2+ . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Purification and characterization of caldesmon 77 : a calmodulin binding protein that interacts with actin filaments from bovine adrenal medulla . ^^^ Caldesmon 150 , a protein composed of the Mr 150 , 000 / 147 , 000 doublet , alternately binds to calmodulin and actin filaments in a Ca2+ dependent `` flip flop ' ' fashion . ^^^ Caldesmon 77 possesses a number of features in common with caldesmon 150 , including flip flop binding to calmodulin and actin filaments depending on the concentration of Ca2+ and crossreactivity with caldesmon 150 specific antibody . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Calcium dependent interaction of actin filaments with actin binding protein in the presence of calmodulin and caldesmon . ^^^ Caldesmon , calmodulin , and actin binding protein of chicken gizzard did not affect the process of polymerization of actin induced by 0 . 1 M KCl . ^^^ Low shear viscosity and flow birefringence measurements revealed that in a system of calmodulin , caldesmon , ABP , and F actin , gelation occurs in the presence of micromolar Ca2+ concentrations , but not in the absence of Ca2+ . ^^^ These results were interpreted by the flip flop mechanism : in the presence of Ca2+ , a calmodulin caldesmon complex is released from actin filaments on which ABP exerts its gelating action . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Chicken gizzard smooth muscle contains two major calmodulin binding proteins : caldesmon ( 11 . 1 microM ; Mr 141 000 ) and myosin light chain kinase ( 4 . 6 microM ; Mr 136 000 ) , both of which are associated with the contractile apparatus . ^^^ Caldesmon lacked myosin light chain kinase and phosphatase activities and did not compete with either myosin light chain kinase or cyclic nucleotide phosphodiesterase ( both calmodulin dependent enzymes ) for available calmodulin , suggesting that calmodulin may have distinct binding sites for caldesmon on the one hand and myosin light chain kinase and cyclic nucleotide phosphodiesterase on the other . ^^^ The phosphorylation and dephosphorylation of caldesmon were further characterized and the Ca2+ / calmodulin dependent caldesmon kinase was purified ; kinase activity correlated with a protein of subunit Mr 93 000 . ^^^ Caldesmon was not a substrate of myosin light chain kinase or phosphorylase kinase , both calmodulin activated protein kinases . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Recent studies raise the possibility that the calcium calmodulin complex may also modulate smooth muscle contractile activity by removing the inhibition imposed by caldesmon , a protein that is bound to the thin ( i . e . , actin containing ) filaments of smooth muscle . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The expression and immunocytochemical localization of three brush border cytoskeletal calmodulin binding proteins , caldesmon , fodrin , and the 110 kDa subunit of the 110 kDa calmodulin complex , have been studied in human intestinal epithelial cells as a function of their ontogenic differentiation . ^^^ This study demonstrates that the developmental pattern of the three calmodulin binding proteins investigated , caldesmon , fodrin and the 110 kDa subunit , parallels the temporal differentiation of human intestinal brush borders and the proximo distal morphological intestinal maturation . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Proteins of 225 and 90 kDa were labeled by antisera against myosin light chain kinase ; 60 and 82 kDa proteins were labeled by antisera against the calmodulin dependent phosphatase and caldesmon , respectively . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Comparison of Ca2+ dependent effects of caldesmon tropomyosin calmodulin and troponin tropomyosin complexes on the structure of F actin in ghost fibers and its interaction with myosin heads . ^^^ Comparison of two types of Ca2+ regulated thin filament , reconstructed in ghost fibers by incorporating either caldesmon gizzard tropomyosin calmodulin or skeletal muscle troponin tropomyosin complex , was performed by polarized microphotometry . ^^^ The results show that in the presence of smooth muscle tropomyosin and calmodulin , caldesmon causes Ca2+ dependent alterations of actin conformation and flexibility similar to those induced by skeletal muscle troponin tropomyosin complex . ^^^ However , whereas troponin in the absence of Ca2+ potentiates the effect of skeletal muscle tropomyosin , caldesmon calmodulin complex inhibits the effect of smooth muscle tropomyosin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Photocrosslinking of calmodulin and / or actin to chicken gizzard caldesmon . ^^^ The two sulfhydryl groups of chicken gizzard caldesmon were specifically labeled with a photoreactive crosslinker , benzophenone maleimide , to study its interactions with calmodulin and / or actin . ^^^ When incubated with F actin caldesmon crosslinks to a single actin monomer ; it can , however , crosslink to up to two calmodulin molecules in the presence , but not in the absence , of Ca2+ . ^^^ Thus caldesmon may have two calmodulin binding sites , each containing , or being near , one of the two thiol residues . ^^^ A calmodulin binding fragment of caldesmon resulting from cyanogen bromide digestion crosslinks to a single calmodulin molecule , also in a Ca2+ dependent manner . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon calmodulin interaction . ^^^ Addition of calmodulin to caldesmon causes a concentration dependent shortwave shift and an increase of fluorescence intensity of caldesmon tryptophan residues . ^^^ The existence of a protein complex is confirmed by the increase of the caldesmon sedimentation coefficient s 0 ( 20 , w ) from 3 . 0 S to 4 . 5 S in the presence of calmodulin . ^^^ These findings allow application of the method of protein intrinsic tryptophan fluorescence for quantitative study of unmodified caldesmon and calmodulin in solution . ^^^ The affinity of the caldesmon calmodulin interaction ( Kass = 1 . 8 10 10 ( 6 ) M 1 , in 0 . 1 M KCl at 25 degrees C ) and Ca2+ requirement ( half maximum binding at 0 . 8 microM Ca2+ ) determined by means of the fluorescence technique are in agreement with previously reported values , thus confirming the validity of the method . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The binding of caldesmon to tropomyosin was regulated by Ca2+ and calmodulin , i . e . , at low ionic strength most of the caldesmon bound to tropomyosin Sepharose 4B was co eluted by adding calmodulin only in the presence of Ca2+ , but not in its absence . ^^^ Actin and calmodulin binding sites on the caldesmon molecule were located in the 38K fragment ( Fujii , T . , Imai , M . , Rosenfeld , G . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , a major calmodulin binding protein , was found to bind smooth muscle myosin . ^^^ Addition of caldesmon to smooth muscle myosin induced the formation of small aggregates of myosin in the absence of Ca2+ calmodulin , but not in the presence of Ca2+ calmodulin . ^^^ Subfragment 1 was not retained by the column , while heavy meromyosin and subfragment 2 were bound to the caldesmon affinity column in the absence of Ca2+ calmodulin but not in its presence . ^^^ It was therefore concluded that the binding site of caldesmon on myosin molecule was the subfragment 2 region and that binding of caldesmon to myosin was abolished in the presence of Ca2+ and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon was originally purified from gizzard smooth muscle as a major calmodulin binding protein which also interacts with actin filaments . ^^^ Considering its abundance , the Ca2+ dependent flip flop binding ability to either calmodulin or actin filaments , and its intracellular localization , caldesmon is expected to be involved in contractile events . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Isolation and characterization of a calmodulin binding fragment of chicken gizzard caldesmon . ^^^ A calmodulin binding portion was separated from chicken gizzard caldesmon by chymotryptic digestion and it was purified through two column chromatography steps on calmodulin Sepharose and Ultrogel AcA 44 . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The cross reacting protein in chicken gizzard smooth muscle had an apparent molecular weight of 140 , 000 and was demonstrated to be caldesmon , a calmodulin and actin binding protein ( Sobue , K . , Y . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon : a calmodulin binding actin regulatory protein . ^^^ The protein caldesmon , originally isolated from smooth muscle tissue where it is the most abundant calmodulin binding protein , has since been shown to have a wide distribution in actin and myosin containing cells where it is localized in sub cellular structures concerned with motility , shape changes and exo or endo cytosis . ^^^ Caldesmon inhibits the activation by actin tropomyosin of myosin MgATPase activity , and the inhibition can be reversed by Ca2+ . calmodulin . ^^^ The abundance of caldesmon , and the Ca2+ regulation of its activity via calmodulin , mean that it is potentially an important intracellular regulator of processes such as smooth muscle contraction , cell motility and secretion . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Arterial caldesmon shares the alternative binding to calmodulin or F actin in a Ca2+ dependent manner and the antigenic determinants with the gizzard protein . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Further , it was found that calmodulin could overcome the inhibitory effects of caldesmon on the above interactions , resulting in contraction . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon is a widely distributed calmodulin and actin binding protein which occurs in different forms depending on the tissue or cell type under examination . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
On the other hand , actin binding proteins , caldesmon and calspectin which also bind to calmodulin , and 36K protein which also binds to calspectin , were examined using antibodies specific for each protein . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Communication between two globular domains of calmodulin in the presence of mastoparan or caldesmon fragment . ^^^ Ca2+ binding to calmodulin was measured in the presence of mastoparan or caldesmon fragment . ^^^ Mastoparan and caldesmon fragment were used as model compounds of enzymes and cytoskeleton proteins , respectively , working as the target of calmodulin . ^^^ Although the Ca2+ bindings of the two globular domains of calmodulin occur independently in the absence of the target peptide ( or proteins ) , mastoparan and caldesmon fragment increased the affinity of Ca2+ and , at the same time , produced the positive cooperative Ca2+ bindings between the two domains . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Under the influence of caldesmon and tropomyosin , calmodulin conferred Ca2+ sensitivity on the filamin induced gelation of actin filaments . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The 145 , 000 and 240 , 000 dalton calmodulin binding bands contained polypeptides that were immunologically similar to caldesmon and to the alpha subunit of the non erythroid spectrin ( fodrin ) respectively . ^^^ Immunocytochemical localization of the three calmodulin binding proteins revealed that , at fetal day 14 , caldesmon and fodrin displayed fluorescence lining the periphery of the epithelial cells , whereas staining with the 110K antisera was very weak . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Here , we demonstrate that one of the cytosolic granule binding proteins with a relative molecular mass ( Mr ) of 70 , 000 ( 70K ) is a form of the calmodulin regulated actin binding protein caldesmon , first isolated from smooth muscle . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The distribution of caldesmon ( a calmodulin binding , F actin interacting protein ; Sobue et al . 1982 ) and actin was studied in the rat thyroid gland by means of light microscopic immunocytochemistry , and the fine structural distribution of actin filaments was examined by use of heavy meromyosin ( HMM ) . ^^^ These results suggest that caldesmon and actin , in conjugation with calmodulin , play a role in the regulation of cellular activity such as exocytosis and endocytosis in the apical portion of the follicle epithelial cell . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , a major calmodulin and actin binding protein of smooth muscle ( Sobue , K . , Muramoto , Y . , Fujita , M . , and Kakiuchi , S . ( 1981 ) Proc . ^^^ A Ca2+ and calmodulin dependent kinase which catalyzed phosphorylation of caldesmon was identified in chicken gizzard ; this kinase is distinct from myosin light chain kinase . ^^^ Caldesmon prepared by calmodulin Sepharose affinity chromatography was contaminated with caldesmon kinase activity and was unable to inhibit actomyosin ATPase activity or superprecipitation . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , a calmodulin binding , F actin interacting protein , is present in aorta , uterus and platelets . ^^^ Caldesmon , a protein originally found in chicken gizzard , was concluded also to be present in bovine aorta , uterus , and human platelets by demonstration of a protein with the following properties : ( a ) Ca2+ dependent calmodulin binding ; ( b ) binding to F actin in such way that the binding was broken on Ca2+ dependent binding of calmodulin ; ( c ) cross reactivity in immune blotting procedures with affinity purified antibody against gizzard caldesmon ; ( d ) similar subunit Mr values on SDS gel to those of gizzard caldesmon . ^^^ A polypeptide of Mr 165 000 that was immunologically distinct from caldesmon but , like caldesmon , bound to calmodulin and F actin in a flip flop fashion , was also demonstrated in aorta and uterus . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In addition , Ca++ seems to inhibit through calmodulin the binding of caldesmon to actin , allowing actin linkage to myosin in a ' flip flop ' fashion . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We propose that actin and tropomyosin are involved in the force producing interaction with myosin , and that this interaction is controlled by a Ca2+ dependent mechanism involving caldesmon , tropomyosin and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Gelsolin ( 0 . 01 : actin ) reduced the inhibition of actomyosin ATPase caused by caldesmon and increased the potency of Ca ( 2+ ) calmodulin in reversing this inhibition . ^^^ Filamin ( 0 . 007 : actin ) also decreased the inhibitory action of caldesmon on actin activated myosin ATPase and also potentiated the reversal of this inhibition by calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caltropin ( CaT ) binds caldesmon ( CaD ) in a Ca ( 2+ ) dependent manner with an affinity higher than that of calmodulin ( CaM ) . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Since inhibition of caldesmon on actin myosin interaction can be overcome by calmodulin and Ca2+ , caldesmon may be involved in the Ca ( 2+ ) dependent regulation in growth cone motility . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Based in part on our results and those of other investigators , we propose that direct Ca ( 2+ ) calmodulin binding to caldesmon or phosphorylation of caldesmon by a Ca ( 2+ ) dependent MAP kinase disinhibits caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
A calmodulin binding protein called `` caldesmon ' ' was purified from chicken gizzard muscle as the major calmodulin binding protein in this tissue . ^^^ The interaction of caldesmon with F actin was abolished by the binding of calmodulin with the caldesmon . ^^^ Because the interaction between caldesmon and calmodulin was Ca2+ dependent but the interaction between caldesmon and F actin was not , Ca2+ acts as a flip flop switch between the formations of two complexes , caldesmon . calmodulin and caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Reconstitution of Ca2+ sensitive gelation of actin filaments with filamin , caldesmon and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In this work , we have used `` isotope edited ' ' Fourier transform infrared spectroscopy to study the interaction of CaM with synthetic peptides resembling the CaM binding domains of myosin light chain kinase ( MLCK ) , constitutive nitric oxide synthase ( cNOS ) , and caldesmon ( CaD ) . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Identification of the functionally relevant calmodulin binding site in smooth muscle caldesmon . ^^^ The C terminal region of smooth muscle caldesmon ( CaD ) interacts with calmodulin ( CaM ) and reverses CaD ' s inhibitory effect on the actomyosin ATPase activity . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The interaction between myosin and F actin requires the enzyme , myosin light chain kinase ( MLCK ) , as well as Ca ( 2+ ) calmodulin and the calmodulin binding protein , caldesmon , which also binds to F actin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In addition to the major regulatory pathway of Ca ( 2+ ) calmodulin myosin light chain kinase , there are other thin filament linked regulatory mechanisms in which Ca ( 2+ ) calmodulin dependent phosphorylation of calponin and caldesmon may be involved . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
In addition , the thin filament associated proteins , caldesmon and calponin , which inhibit the actin activated MgATPase activity of smooth muscle myosin ( the cross bridge cycling rate ) , appear to be regulated by calmodulin , either by the direct binding of Ca2+ / calmodulin or indirectly by phosphorylation catalysed by Ca2+ / calmodulin dependent protein kinase 2 . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Interaction of smooth muscle caldesmon with calmodulin mutants . ^^^ The interaction of avian smooth muscle caldesmon with calmodulin ( CaM ) was investigated by studying the ability of selected mutant calmodulins to induce fluorescence changes in caldesmon . ^^^ Affinity of calmodulin to caldesmon was decreased 2 4 times by point mutation G33V CaM , double mutation E84K / E120K CaM , deletion of residues 82 84 , and by cluster mutations DEE 118 120 > KKK or EEE 82 84 > KKK . ^^^ Mutations of the first ( E31A CaM ) and the second ( E67A CaM ) calcium binding sites reduced the affinity of calmodulin to caldesmon by at least 5 fold ; in addition these calmodulin mutants exhibited smaller changes in the fluorescence spectra of caldesmon . ^^^ Simultaneous mutation of the two negatively charged clusters of calmodulin EEE 82 84 > KKK and DEE 118 120 > KKK resulted in a more than 15 fold decrease in the affinity of calmodulin for caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Phosphorylation of rat non muscle caldesmon by cdc 2 kinase causes reduction in most of caldesmon ' s properties , including caldesmon ' s binding to actin , myosin , and calmodulin , as well as its inhibition of actomyosin ATPase . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The calmodulin binding domain of caldesmon binds to calmodulin in an alpha helical conformation . ^^^ The binding of calcium calmodulin ( CaM ) to caldesmon ( CaD ) contributes to the regulation of smooth muscle contraction . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Location of two contact sites between human smooth muscle caldesmon and Ca ( 2+ ) calmodulin . ^^^ We measured Ca ( 2+ ) calmodulin binding to expressed human caldesmon fragments by three techniques : tryptophan fluorescence enhancement , change in fluorescence of TA calmodulin , and cosedimentation with calmodulin Sepharose . ^^^ Ca ( 2+ ) calmodulin bound with similar affinity to peptide M 73 ( C714SMWEKGNVFSSPGF727 , N terminus of domain 4b ) , to all the fragments of caldesmon containing this peptide , and also to H 9 ( Thr 726 Val793 ) , which did not contain this peptide ( Kd = 0 . 2 0 . 8 microM ) . ^^^ We conclude that Ca ( 2+ ) calmodulin binds at two sites on caldesmon ; site A is the sequence 715MWEKGNVFS723 previously identified by Zhan et al . ( Zhan , Q . , Wong , S . ^^^ Ca ( 2+ ) calmodulin binding at site B is coupled to reversal of caldesmon inhibition of actin tropomyosin activated myosin MgATPase , while calmodulin binding at site A has no detectable function . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
This could explain the effects of calmodulin and phosphorylation on the caldesmon phospholipid interaction described earlier . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Precise identification of the regulatory F actin and calmodulin binding sequences in the 10 kDa carboxyl terminal domain of caldesmon . ^^^ The precise location of the regulatory F actin and calmodulin binding sites in the COOH terminal sequence Trp 659 Pro756 of gizzard caldesmon was investigated by subjecting the corresponding 10 kDa CNBr fragment , characterized earlier ( Bartegi , A . , Fattoum , A . , Derancourt , J . , and Kassab , R . ( 1990 ) J . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Phosphorylation did not significantly affect the interaction of caldesmon with Ca ( 2+ ) calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Myosin 1 from mammalian smooth muscle is regulated by caldesmon calmodulin . ^^^ Caldesmon , a calmodulin / actin binding protein , inhibits the actin activated ATPase activity of myosin 1 . ^^^ When caldesmon is bound to actin , Ca2+ sensitivity is increased to 80 % in the presence of calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The binding of the 20 kDa fragments to actin is totally reversed by Ca ( 2+ ) calmodulin and , like intact caldesmon , the 20 kDa fragments are competitive with the binding of myosin subfragments to actin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
These studies suggest that calponin binds CaM with 80 fold lower affinity than myosin light chain kinase and that calponin associates with CaM much slower than it associates with caldesmon or myosin light chain kinase . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Interaction of smooth muscle caldesmon with calmodulin , troponin C , S 100 protein and 67 kDa calcimedin was analyzed . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The enhancement of release by calmodulin was specific to calmodulin : bovine serum albumin , actin , and caldesmon had no such effect . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Ca ( 2+ ) calmodulin abolished the stimulatory effect of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Addition of calcium and calmodulin partially released caldesmon from actin filaments . ^^^ PSK dependent release of caldesmon was also observed in the presence of calcium and calmodulin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We further presented a few data which suggest that calponin may exert regulatory activity toward myosin in quite a different way from caldesmon , another smooth muscle protein that binds to myosin , actin , and calmodulin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Ca2+ , caldesmon , and myosin light chain kinase exchange with calmodulin . ^^^ CaM undergoes a large fluorescence increase when it binds myosin light chain kinase ( MLCK ) and caldesmon ( CaD ) , but little fluorescence change when it binds CaM antagonists or Ca2+ . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
An improved rotary shadowing technique enabled us to visualize chicken gizzard caldesmon ( CaD ) and its complexes with one or two covalently linked calmodulin ( CaM ) molecules by electron microscopy . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Binding of PS at this site results in displacement of calmodulin from its complex with caldesmon . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
CDh , 606C , and 658C inhibited actin tropomyosin activated myosin ATPase , with maximal inhibition correlated with 1 caldesmon bound / 14 actins , and inhibition was reversed by Ca ( 2+ ) calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
A series of C terminal deletion mutants of chicken gizzard smooth muscle caldesmon ( CaD ) were made using a polymerase chain reaction cloning strategy and a baculovirus expression system , and the precise locations of the functional domains of CaD involved in the regulation of actomyosin ATPase and the binding of actin , tropomyosin , and calmodulin were analyzed . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Titrations of pyrene caldesmon with actin , heavy meromyosin , and calmodulin resulted in a decrease in excimer fluorescence . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon is an actin , calmodulin , tropomyosin , and myosin binding protein implicated in the regulation of actomyosin interactions . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Multiple sited interaction of caldesmon with Ca ( 2+ ) calmodulin . ^^^ The binding of Ca ( 2+ ) and Ba ( 2+ ) calmodulin to caldesmon and its functional consequence was investigated with three different calmodulin mutants . ^^^ When Ca2+ was replaced by Ba2+ the affinity of calmodulin for caldesmon was further reduced . ^^^ The ability of Ca ( 2+ ) calmodulin to release caldesmon ' s inhibition of the actin tropomyosin activated myosin ATPase was virtually abolished by mutation of phenylalanine 92 to alanine or by replacing Ba2+ for Ca2+ in native calmodulin . ^^^ Ca2+ calmodulin produced a broadening in the signals of the NMR spectrum of the 10 kDa Ca ( 2+ ) calmodulin binding C terminal fragment of caldesmon arising from tryptophans 749 and 779 and caused an enhancement of maximum tryptophan fluorescence of 49 % and a 16 nm blue shift of the maximum . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Cleavage of caldesmon and calponin by calpain : substrate recognition is not dependent on calmodulin binding domains . ^^^ The calmodulin binding proteins , caldesmon and calponin , are cleaved by both major isoforms of calpain in vitro . ^^^ In order to demonstrate , unequivocally , that substrate recognition does not require an interaction between calpain and a substrate ' s calmodulin binding domain , recombinant , full length caldesmon and a mutant lacking the calmodulin binding domain were tested as substrates for calpain in the presence and absence of calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Utilization of troponin C as a model calcium binding protein for mapping of the calmodulin binding sites of caldesmon . ^^^ Troponin C , a structural analogue of calmodulin , was used for mapping the calmodulin binding sites of caldesmon . ^^^ The apparent Kd values for the formation of the caldesmon calcium binding protein complex as determined by native gel electrophoresis were 0 . 5 , 1 . 2 and 3 . 9 microM for calmodulin , rabbit skeletal muscle troponin C and bovine cardiac troponin C respectively . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
NMR studies of caldesmon calmodulin interactions . ^^^ The binding of the calcium regulatory protein calmodulin ( CaM ) to caldesmon ( CaD ) contributes to the regulation of smooth muscle contraction . ^^^ Two regions of caldesmon have been identified as putative calmodulin binding domains . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Three different peptides , corresponding to the CaM binding domain of skeletal muscle myosin light chain kinase ( MLCK ) , CaM dependent cyclic nucleotide phosphodiesterase ( PDE ) , and smooth muscle caldesmon ( CaD ) , were examined and show different reductions in their affinities toward CaM . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
If only the central segment is present ( H 2 , H2+12 ) , the actin tropomyosin caldesmon peptide complex is not inhibitory , and its properties resemble actin tropomyosin caldesmon Ca2+ 10 calmodulin . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Mapping of contact sites in the caldesmon calmodulin complex . ^^^ The interaction of intact calmodulin and its four tryptic peptides with deletion mutants of caldesmon was analysed by native gel electrophoresis , fluorescence spectroscopy and zero length cross linking . ^^^ The N terminal peptides of calmodulin ( TR1C and TR2E ) could be cross linked to intact caldesmon and its deletion mutants H 2 and H 9 . ^^^ The similarity in the primary structures of sites A and B ' of caldesmon and our measurements of the affinities of H 2 and H 9 to calmodulin and its peptides strongly indicate an orientation of the protein complex where sites A and B ' interact with the N terminal domain of calmodulin , whereas site B interacts with the C terminal domain of calmodulin . ^^^ The spatial organization of contact sites in the caldesmon calmodulin complex agrees with the earlier proposed two dimensional model of interaction of the two proteins [ Huber , El Mezgueldi , Grabarek , Slatter , Levine and Marston ( 1996 ) Biochem . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Functional and structural relationship between the calmodulin binding , actin binding , and actomyosin ATPase inhibitory domains on the C terminus of smooth muscle caldesmon . ^^^ Multiple functional domains responsible for calmodulin ( CaM ) binding and actin binding / actomyosin ATPase inhibition are present in the region between residues 598 756 of the chicken gizzard smooth muscle caldesmon ( CaD ) molecule . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
To determine the PS binding sites of caldesmon , we have made use of synthetic peptides covering the two C terminal calmodulin binding sites and a recombinant fragment corresponding to the N terminal end of the C terminal domain that contains an amphipathic helix . ^^^ The results showed that both calmodulin binding sites of caldesmon were able to interact with PS . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Melittin was also found to promote both the aggregation of the purified 24 kDa C terminal fragment of the kinase and its analogue telokin , as well as of myosin light chains , but had no effect on the solubility of bovine serum albumin , caldesmon , or calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , a calmodulin and actin binding protein , is a molecular marker of the phenotypic change in smooth muscle cells . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Biochemical investigations showed common properties of this protein with animal caldesmon it binds to actin and , in a Ca ( 2+ ) dependent manner , to calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
When calmodulin is added , the inhibition of fascin actin interaction by caldesmon and TM becomes Ca2+ dependent because Ca2+ / calmodulin blocks actin binding of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We have combined functional studies with expression and mutagenesis of caldesmon and with structural methods including 10 ray crystalography of tropomyosin caldesmon crystals , electron microscopy and helical reconstruction of actin tropomyosin caldesmon complexes and high resolution nuclear magnetic resonance spectroscopy of the C terminus of caldesmon in interaction with actin and calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon , a calmodulin or actin binding protein , is a molecular marker of differentiation in smooth muscle cells and has recently been shown by us to be a good marker of mesangial cell activation in IgA nephropathy patients . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Under the same conditions , calmodulin and tropomyosin ( known to bind to the C terminus of caldesmon ) produced substantial changes in these spectral parameters . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The conserved regions of all isoforms contain caldesmon ' s properties such as binding to actin , tropomyosin , Ca ( 2+ ) calmodulin , myosin and phospholipids . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
S 100 reverses the inhibitory action of intact caldesmon and its deletion mutants 606C ( residues 606 756 ) and H 9 ( residues 669 737 ) as effectively as calmodulin . ^^^ Although monomeric ( calmodulin , troponin C ) and dimeric ( S 100 ) Ca binding proteins have different sizes and structures they interact with caldesmon in a very similar fashion . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Characterisation of the effects of mutation of the caldesmon sequence 691glu trp leu thr lys thr 696 to pro gly his tyr asn asn on caldesmon calmodulin interaction . ^^^ Cg 1 bound Ca2+ calmodulin with ( 1 / 7 ) th of the affinity as compared to 658C or whole caldesmon . ^^^ We conclude that the interaction of calmodulin with this caldesmon sequence is crucial for the reversal of caldesmon inhibition of actin tropomyosin activation of myosin ATPase . ^^^ The results are interpreted in terms of multisite attachment of actin and Ca2+ calmodulin to overlapping sequences in caldesmon domain 4b . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Calmodulin remains extended upon binding to smooth muscle caldesmon : a combined small angle scattering and fourier transform infrared spectroscopy study . ^^^ We show that calmodulin ( CaM ) has an extended conformation in its complexes with sequences from the smooth muscle thin filament protein caldesmon ( CaD ) by using small angle 10 ray and neutron scattering with contrast variation . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Both CaM isoforms supported near maximal activation of CaM dependent protein kinase 2 ( CaM KII ) , but SCaM 4 exhibited approx . 12 fold higher K ( act ) than SCaM 1 for CaM KII phosphorylation of caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The contents of actin and calponin were increased by AF64A , whereas those of myosin , calmodulin and caldesmon were not affected . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We studied the Ca ( 2+ ) capture ability of follicular dendritic cells ( FDCs ) in tonsillar secondary lymphoid follicles ( LFs ) and the expression of six Ca ( 2+ ) binding proteins ( CBPs ) , caldesmon , S 100 protein , calcineurin , calbindin D , calmodulin , and annexin 6 in LFs of various lymphoid tissues and caldesmon and S 100 protein in neoplastic follicles of follicular lymphomas . ^^^ Immunoelectron microscopic staining of FDCs was classified into two patterns : caldesmon was distributed in the peripheral cytoplasm like a belt ; S 100 protein , calcineurin , calbindin D , and calmodulin were distributed diffusely in the cytosol . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon is known to inhibit the ATPase activity of actomyosin in a Ca ( 2+ ) calmodulin regulated manner . ^^^ The effects of caldesmon are blocked by the ionophore A 23187 , thapsigargin , and membrane depolarization , presumably because of the ability of Ca ( 2+ ) calmodulin or Ca ( 2+ ) S 100 proteins to antagonize the inhibitory function of caldesmon on actomyosin contraction . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Mass spectroscopy data show that stoichiometric phosphorylation occurs at Ser ( 657 ) and Ser ( 687 ) abutting the calmodulin binding sites A and B of chicken gizzard caldesmon , respectively . ^^^ PAK phosphorylation reduces binding of caldesmon to calmodulin by about 10 fold whereas binding of calmodulin to caldesmon partially inhibits PAK phosphorylation . ^^^ We conclude that PAK phosphorylation of caldesmon at the calmodulin binding sites modulates caldesmon inhibition of actin myosin ATPase activity and may , in concert with the actions of Rho kinase , contribute to the regulation of Ca ( 2+ ) sensitivity of smooth muscle contraction . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon ( CaD ) is a major calmodulin and actin binding protein distributed in smooth muscle cells ( SMC ) and nonmuscle cells . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Tryptophan steady state fluorescence from peptides encompassing the CaM binding domains of the target proteins myosin light chain kinase ( MLCK ) , cyclic nucleotide phosphodiesterase ( PDE ) and caldesmon site A and B ( CaD A , CaD B ) , and the model peptide melittin showed Ca ( 2+ ) dependent blue shifts in their maximum emission wavelength when complexed with wild type CaM . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
This study was undertaken to determine if caldesmon , calmodulin , S100beta , and neurocalcin delta were present in chick forebrain neurons , and if so , to investigate the interactions of these proteins in the presence of different concentrations of calcium . 2 . ^^^ Our data show that caldesmon and three calcium binding proteins ( S100beta , calmodulin , and neurocalcin 3 ) are localized in growth cones and neurites of chick forebrain neurons in culture . ^^^ S100beta binds with greater affinity than calmodulin to caldesmon , and its ability to bind to caldesmon is regulated by neurocalcin delta . 4 . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
It is suggested that calponin ' s role , in the presence of Ca ( 2+ ) and calmodulin , is that of a modulator and that caldesmon , a molecule that competes with calponin for actin binding sites , is in a position in which it can switch on and off Ca ( 2+ ) dependent contractility and relaxation . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
GS17C , a previously characterized peptide , from the calmodulin binding domain of caldesmon was tagged with iodoacetyl nitrobenz 2 oxa 1 , 3 diazole ( NBD ) or , as a negative control , with iodoacetylfluorescein isothiocyanate . ^^^ These results suggest that the total unbound intracellular calmodulin levels may be sufficient to regulate the activity of caldesmon and , furthermore , that phosphorylation of protein kinase C substrates may increase the level of available calmodulin in living smooth muscle cells . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Thermodynamic parameters of interactions of calcium saturated calmodulin ( Ca ( 2+ ) CaM ) with melittin , C terminal fragment of melittin , or peptides derived from the CaM binding regions of constitutive ( cerebellar ) nitric oxide synthase , cyclic nucleotide phosphodiesterase , calmodulin dependent protein kinase 1 , and caldesmon ( CaD A , CaD A * ) have been measured using isothermal titration calorimetry . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Actin , myosin , and calmodulin , not surprisingly , were confirmed for all three chromatophore types of the two fishes , but the presence of caldesmon and calponin , both characteristic proteins of smooth muscle fibers , represents a new discovery . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The interaction of caldesmon with different Ca2+ binding proteins has been analyzed , and it is supposed that one of the conformers of calmodulin might be an endogenous regulator of caldesmon . ^^^ The central helix of calmodulin is supposed to be located near the single Cys residue in the C terminal domain of caldesmon . ^^^ The N terminal globular domain of calmodulin interacts with sites A and B ' of caldesmon , whereas the C terminal globular domain of calmodulin binds to site B of caldesmon . ^^^ The complex of calmodulin and caldesmon is very flexible ; therefore , both parallel and antiparallel orientation of polypeptide chains of the two proteins is possible in experiments with short fragments of caldesmon and calmodulin . ^^^ The length , flexibility , and charge of the central helix of calmodulin play an important role in its interaction with caldesmon . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Caldesmon binding to actin is regulated by calmodulin and phosphorylation via different mechanisms . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
We also have found that the inhibition of the binding between actin and caldesmon either by Ca ( 2+ ) / calmodulin or by phosphorylation with cdc 2 kinase reverses the inhibitory effect of caldesmon on Arp2 / 3 induced actin polymerization . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Thrombin induced ERK dependent caldesmon phosphorylation ( Ser 789 ) was inhibited by either KN 93 , a specific CaM kinase 2 inhibitor , or U 0126 , an inhibitor of MEK activation . ^^^ These results strongly suggest the involvement of CaM kinase 2 and ERK activities in thrombin mediated caldesmon phosphorylation and both contractile and barrier regulation . . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Natively unfolded C terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
These examples include both more recently described signaling proteins , such as p 53 , alpha synuclein , HMGA , the Rieske protein , estrogen receptor alpha , chaperones , GCN 4 , Arf , Hdm 2 , FlgM , measles virus nucleoprotein , RNase E , glycogen synthase kinase 3beta , p 21 ( Waf1 / Cip1 / Sdi1 ) , caldesmon , calmodulin , BRCA 1 and several other intriguing proteins , as well as historical prototypes for signaling , regulation , control and molecular recognition , such as the lac repressor , the voltage gated potassium channel , RNA polymerase and the S 15 peptide associating with the RNA polymerase S protein . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
Here we report the identification of the actin and calmodulin binding protein caldesmon ( CALD 1 ) as a novel K cyclin . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
The mean SS level was higher in cancer adjacent mucosa ( CAM , 0 2 cm from the tumor ) than in cancer distant mucosa ( CDM , about 5 cm from the tumor ) , and in CAM without atypical hyperplasia than in such mucosa with different grades of atypical hyperplasia ( P < 0 . 01 ) . ^^^ Both the mean SS cell number and total positive degree were very significantly higher in CAM than CDM ( P < 0 . 01 ) . ^^^
Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
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Interacting proteins: Q05682 and P62158	Pubmed	SVM Score :0.0
NA