Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.51445964 |
We propose that calmodulin regulates casein kinase 2 phosphorylation of neuromodulin by binding to neuromodulin and sterically hindering the interaction of casein kinase 2 with its phosphorylation sites on neuromodulin . . 0.51445964^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.55119697 |
In the yeast based cloning system , the only strong interaction that was detected between GAP 43 and the calcium effector protein , calmodulin ( CaM ) . 0.55119697^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Nonisotopic in situ hybridization techniques were used to define the subcellular localization of representative mRNAs including beta tubulin , low molecular weight neurofilament protein ( NF 68 ) , high molecular weight microtubule associated protein ( MAP 2 ) , growth associated protein 43 ( F1 / GAP43 ) , the alpha subunit of calcium / calmodulin dependent protein kinase 2 ( alpha CaMII kinase ) , and poly ( A+ ) mRNA . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Among them , GAP 43 ( growth associated protein 43 ) like proteins interact with PtdIns ( 4 , 5 ) P ( 2 ) in a Ca ( 2+ ) / calmodulin and PKC ( protein kinase C ) regulated manner , and function as intrinsic determinants of motility and anatomical plasticity . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The intracellular effector CaM ( calmodulin ) can reverse this binding on a wide variety of proteins , including MARCKS ( myristoylated alanine rich C kinase substrate ) , GAP 43 ( growth associated protein 43 , also known as neuromodulin ) , gravin , GRK 5 ( G protein coupled receptor kinase 5 ) , the NMDA ( N methyl D aspartate ) receptor and the ErbB family . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Enhanced activation of CaM kinase by PKC may result from PKC mediated phosphorylation of calmodulin binding proteins , such as neuromodulin and MARCKS , and the subsequent increase in the availability of previously bound calmodulin for activation of CaM kinase . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
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 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
In this review , we will discuss research which has defined several of the functional domains of neuromodulin , including its phosphorylation sites , calmodulin binding domain , membrane binding domain and growth cone targeting domain . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Included in these analyses was a tryptophan containing peptide analog of the calmodulin binding domain of neuromodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Four highly basic putative calmodulin binding sites in the Ca ( 2+ ) dependent phosphatidylserine binding region of the heavy chain were identified based on the similarity in their sequence to the calmodulin and phosphatidylserine binding site of neuromodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Characterization of the calmodulin binding domain of neuromodulin . ^^^ Phosphorylation of neuromodulin decreases its affinity for calmodulin , suggesting that neuromodulin may function to bind and concentrate calmodulin at specific sites within neurons , releasing calmodulin locally in response to phosphorylation by protein kinase C ( Alexander , K . ^^^ These hydrophobic interactions may be disrupted by the introduction of negative charge at serine 41 , and thereby regulate the neuromodulin / calmodulin binding interactions . ^^^ The sensitivity of the neuromodulin / calmodulin binding interaction to negative charge at serine 41 was determined by substitution of serine 41 with an aspartate or an asparagine residue . ^^^ We conclude that protein kinase C phosphorylation of neuromodulin abolishes calmodulin binding by introducing negative charges within the calmodulin binding domain at a position adjacent to the phenylalanine . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Identification of a consensus amino acid sequence between neurogranin and neuromodulin ( GAP 43 ) that corresponds to the protein kinase C phosphorylation site and the calmodulin binding domain . ^^^ Evidence was obtained suggesting that neurogranin binds to calmodulin in the absence of Ca2+ , a feature that also characterizes neuromodulin . ^^^ We propose that the amino acid sequence shared by neurogranin and neuromodulin reflects a functional relationship between these two proteins and that the consensus sequence represents a conserved PKC phosphorylation site and a calmodulin binding domain that characterizes a class of brain specific PKC substrates . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The interactions of the brain specific calmodulin binding protein kinase C substrate , neuromodulin ( GAP 43 ) , with membrane phospholipids . ^^^ The interaction of the brain specific calmodulin binding protein kinase C ( PKC ) substrate , neuromodulin ( GAP 43 ) , with membrane phospholipids was studied . ^^^ Comparison of the binding of neuromodulin to acidic phospholipids with that of neurogranin , a newly characterized calmodulin binding PKC substrate ( Baudier J . , Deloulme , J . ^^^ In the absence of calmodulin , binding of neuromodulin to phosphatidylserine at low concentration parallels its phosphorylation by PKC , suggesting that formation of a ternary complex between neuromodulin , phosphatidylserine , and PKC is required for optimum neuromodulin phosphorylation . ^^^ In the presence of calmodulin , the binding of neuromodulin to phosphatidylserine is inhibited , resulting in total inhibition of neuromodulin phosphorylation . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
P 57 or neuromodulin ) could allow it to sequester a large fraction of calmodulin to the submembranous regions , and to release free calmodulin in response to protein kinase C activation . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Regulation of free calmodulin levels by neuromodulin : neuron growth and regeneration . ^^^ Neuromodulin is a neurospecific calmodulin binding protein that is implicated in neurite extension , axonal elongation and long term potentiation . ^^^ Yuechueng Liu and Daniel Storm propose that neuromodulin binds and concentrates calmodulin on growth cone membranes and that stimulation of protein kinase C releases high local concentrations of calmodulin in the growth cone . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Neuromodulin ( also called GAP 43 , G 50 , F 1 , pp 46 ) , a neural specific calmodulin binding protein , is a major protein kinase C substrate found in developing and regenerating neurons . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The CaM binding protein neuromodulin , which demonstrates a decreased affinity for CaM in the presence of Ca2+ and when phosphorylated by protein kinase C , was present in both membranes and cytosol of SK N SH cells . ( ABSTRACT TRUNCATED AT 400 WORDS ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Murine cDNA that encodes neuromodulin , a neurospecific calmodulin binding protein , was inserted into the plasmid pKK 223 3 for expression in Escherichia coli . ^^^ The recombinant neuromodulin and neuromodulin purified from bovine brain had similar , but not identical , affinities of calmodulin , indicating that the palmitylation of the protein that occurs in animal cells is not crucial for calmodulin interactions . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Neuromodulin ( P 57 , GAP 43 , B 50 , F 1 ) is a neurospecific calmodulin binding protein that is phosphorylated by protein kinase C . ^^^ Phosphorylation by protein kinase C has been shown to abolish the affinity of neuromodulin for calmodulin [ Alexander , K . ^^^ Toward this end , it was demonstrated that recombinant neuromodulin purified from Escherichia coli and bovine neuromodulin were phosphorylated with similar Km values and stoichiometries and that protein kinase C mediated phosphorylation of both proteins abolished binding to calmodulin Sepharose . ^^^ The serine in this peptide corresponds to position 41 of the entire protein , which is adjacent to or contained within the calmodulin binding domain of neuromodulin . ^^^ We conclude that serine 41 is the protein kinase C phosphorylation site of neuromodulin and that phosphorylation of this amino acid residue blocks binding of calmodulin to neuromodulin . ( ABSTRACT TRUNCATED AT 250 WORDS ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Regulation of free calmodulin levels in neurons by neuromodulin : relationship to neuronal growth and regeneration . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The interaction of apocalmodulin ( apoCaM ) with a peptide ( Neurop ) based on the primary sequence of the calmodulin binding domain of neuromodulin has been studied by nuclear magnetic resonance ( NMR ) methods . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Neuromodulin ( p 57 , GAP 43 , F 1 , B 50 ) is a major neural specific , calmodulin binding protein found in brain , spinal cord , and retina that is associated with membranes . ^^^ Phosphorylation of neuromodulin by protein kinase C causes a significant reduction in its affinity for calmodulin ( Alexander , K . ^^^ It has been proposed that neuromodulin may function to bind and concentrate calmodulin at specific sites within neurons and that activation of protein kinase C causes the release of free calmodulin at high concentrations near its target proteins . ^^^ One of these phosphatases , which represented approximately 60 % of the total neuromodulin phosphatase activity , was tentatively identified as calcineurin by its requirement for Ca2+ and calmodulin ( CaM ) and inhibition of its activity by chlorpromazine . ^^^ Dephosphorylation of neuromodulin by calcineurin was stimulated 50 fold by calmodulin in the presence of micromolar free Ca2+ . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Identification and characterization of the calmodulin binding domain of neuromodulin , a neurospecific calmodulin binding protein . ^^^ Neuromodulin ( formerly designated P 57 ) is an abundant , neural specific , calmodulin binding protein which exhibits higher affinity for calmodulin in the absence of free Ca2+ than in the presence of free Ca2+ . ^^^ In this study a series of proteolytic fragments of neuromodulin were systematically screened for calmodulin Sepharose binding activity . ^^^ A 9 amino acid fragment , designated M 1 C1 and having the sequence RGHITRKKL , was identified as the putative CaM binding domain of neuromodulin . ^^^ Anti FP 57 Phe antibody binding to neuromodulin was inhibited by preincubation of antibodies with excess FP 57 Phe . 125I CaM gel overlay of neuromodulin was inhibited by anti FP 57 Phe antibodies . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Neuromodulin ( GAP 43 ) can regulate a calmodulin dependent target in vitro . ^^^ The calmodulin binding polypeptide neuromodulin ( GAP 43 ) was tested in vitro for its ability to modulate a typical calmodulin target , the enzyme nitric oxide synthase . ^^^ The results from these in vitro studies have indicated that neuromodulin has the ability to affect the activation of a calmodulin dependent enzyme at levels of the polypeptide that exist in neurons . ^^^ Since the inhibition of enzyme activity appeared to be occurring through the interaction of neuromodulin with calmodulin , it seems likely that neuromodulin has a general ability to impede activation of calmodulin dependent targets . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
By immunological methods and sequence comparison , we have found that p 68 possesses a region of sequence similarity to the conserved protein kinase C phosphorylation site and calmodulin binding domain ( also known as the IQ domain ) of the neural specific proteins neuromodulin ( GAP 43 ) and neurogranin ( RC 3 ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
GAP 43 ( growth associated protein of 43 kDa ; also known as neuromodulin , P 57 , B 50 and F 1 ) is a neuronal calmodulin binding protein and a major protein kinase C ( PKC ) substrate in mammalian brain . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Differential responses of protein kinase C substrates ( MARCKS , neuromodulin , and neurogranin ) phosphorylation to calmodulin and S 100 . ^^^ Phosphorylation of three physiological substrates of protein kinase C ( PKC ) , MARCKS , neuromodulin ( Nm ) , and neurogranin ( Ng ) , was analyzed to determine their relative efficacy as substrates of PKC alpha , beta , and gamma and sensitivities to inhibition by calmodulin ( CaM ) and S 100 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Neuromodulin ( GAP 43 ) is a neurospecific calmodulin binding protein that is targeted to neuronal growth cones via fast axonal transport by an undefined mechanism . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The 50 kDa protein , which bound to calmodulin in the presence of Ca2+ , was more prominent in cells ( N1E 115 and HTB 10 ) with less MARCKS , whereas neuromodulin ( GAP 43 ) was detected in N1E 115 and HTB 11 cells only . ^^^ These results indicate that MARCKS , neuromodulin , and other calmodulin binding protein kinase C substrates exhibit distinct levels of expression in cultured neurotumor cell lines . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
This inhibitory effect of calmodulin was dose dependent and much stronger than its inhibitory effect to the phosphorylation of neuromodulin ( GAP 43 ) with protein kinase C . ^^^ The dissociation constant of NAP 22 and calmodulin obtained using the fluorescence change of dansyl labeled calmodulin was much lower than that of neuromodulin and calmodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Neuromodulin ( GAP 43 ) is a neurospecific calmodulin binding protein which is implicated in neuronal growth and regeneration . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The interaction of apocalmodulin ( apoCaM ) with a peptide ( Neurop ) based on the primary sequence of the calmodulin binding domain of neuromodulin has been studied by fluorescence spectroscopy . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Camstatins are peptide antagonists of calmodulin based upon a conserved structural motif in PEP 19 , neurogranin , and neuromodulin . ^^^ PEP 19 is a 7 . 6 kDa neuron specific protein , which contains a motif similar to the calmodulin binding domains of neuromodulin ( GAP 43 ) and neurogranin ( RC 3 ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The solution , micelle , and membrane bound structure of a peptide based on the protein kinase C and calmodulin binding domain of neuromodulin was studied using a combination of NMR , EPR , and circular dichroism . ^^^ The membrane bound structure of this peptide was investigated with EPR by synthesizing a series of spin labeled peptides based on the protein kinase C and calmodulin binding domain of neuromodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
EPR spectroscopy was used to examine protein protein interactions between calmodulin and spin labeled peptides based on the protein kinase C substrate domains of the myristoylated alanine rich C kinase substrate ( MARCKS ) and neuromodulin . ^^^ For the 17 residue neuromodulin derived peptide , which is Ca2+ independent in its binding to calmodulin , oxygen collision rates demonstrate that one helical face of this peptide interacts strongly with calmodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Calcium vector protein target ( CaVPT ) , a 26 kDa endogenous target of calcium vector protein from Amphioxus ( CaVP ) , contains three distinct regions : a N terminal Pro Ala Lys rich motif , segment 36 50 displaying sequence similarity to the calmodulin binding site in neuromodulin and neurogranin where they are designated as the IQ domain ; and two immunoglobulin like folds . ^^^ Two main conclusions can be drawn from this study : 1 ) the regulation of interaction between CaVP and CaVPT is very similar to the mechanism observed in the complex between neuromodulin or neurogranin and calmodulin ; 2 ) in spite of this similarity the entire CaVP binding site is not restricted to the IQ domain ; in addition the Pro Ala Lys rich motif may be necessary for high affinity binding to CaVP . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Analysis of the role of calmodulin binding and sequestration in neuromodulin ( GAP 43 ) function . ^^^ Here we analyze the role of calmodulin binding by neuromodulin in these responses . ^^^ In cells expressing wild type neuromodulin , a complex with calmodulin that is sensitive to intracellular calcium and phosphorylation is localized to the plasma membrane . ^^^ Transfection of several mutant forms of neuromodulin shows that the effects of this protein on secretion are dependent on both calmodulin binding and association with the plasma membrane . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
A growing family of proteins is regulated by protein kinase C and calmodulin through IQ domains , a regulatory motif originally identified in neuromodulin ( Alexander , K . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
State specific antibodies were used to measure the levels of site 3 phospho synapsin 1 , phosphorylated by CaM kinase 2 , and phospho Ser 41 neuromodulin , phosphorylated by protein kinase C , in incubated striatal S 1 fractions and synaptosomes . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Peptides derived from the membrane and calmodulin binding domains of the myristoylated alanine rich C kinase substrate and neuromodulin were previously found to be in extended conformations ; however , side chains for these peptides penetrated the membrane solution interface . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Previously , sequence analysis of Sp 17 revealed that Sp 17 amino acids 108 137 were 52 % identical to the calmodulin binding domain of neuromodulin and contained an IQ motif found in other calmodulin binding proteins . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
These substrates include the CaM storage proteins ( neurogranin , neuromodulin ) , the membrane associated MARCKS ( myristoylated alanine rich C kinase substrate ) protein , the NMDA receptor RI subunit and the autoinhibitory domain of the plasma membrane Ca2+ pump . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Small proteins that modulate calmodulin dependent signal transduction : effects of PEP 19 , neuromodulin , and neurogranin on enzyme activation and cellular homeostasis . ^^^ Neuromodulin ( GAP 43 ) , neurogranin ( RC 3 ) , and PEP 19 are small acid stable proteins that bind calcium poor calmodulin through a loosely conserved IQ motif . ^^^ Although neuromodulin , neurogranin , and PEP 19 were early representatives of the small IQ motif containing protein family , newer examples have come to light that expand the number of cellular systems through which the IQ peptide / calmodulin interaction could regulate biological processes including gene transcription . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The relationship between the free Ca2+ concentration and the apparent dissociation constant for the complex between calmodulin ( CaM ) and the neuromodulin IQ domain consists of two phases . ^^^ Release of CaM from the neuromodulin IQ domain therefore appears to be promoted over a relatively narrow range of free Ca2+ concentrations . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
GAP 43 ( B 50 , F 1 , pp 46 ) is a calmodulin binding protein which is specific to the nervous system and also a substrate for the protein kinase C . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Does GAP 43 support axon growth by increasing the axonal transport velocity of calmodulin . ^^^ We propose that one consequence of this increased synthesis may be the delivery of calmodulin like proteins to the distal portions of the growing axon at an increased velocity ; this is because calmodulin , which is transported slowly in mature intact axons , can bind to GAP 43 , which is transported rapidly . ^^^ The release of calmodulin from GAP 43 would be regulated by phosphorylation by protein kinase C . ^^^ This hypothetical carrier mechanism is consistent with the phosphorylation pattern , calmodulin binding , transport velocity , and growth association of GAP 43 , and suggests an explanation for the specific importance of newly synthesized GAP 43 in supporting axon growth . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
RC 3 and its bovine homolog neurogranin / B 50 immunoreactive C kinase substrate ( BICKS ) contain overlapping sites for protein kinase C phosphorylation and calmodulin binding that resemble those of the presynaptic 43 kDa growth associated protein ( GAP 43 ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Elevated level of neuronal ( GAP 43 , NCAM , protein kinase C , calmodulin ) and protooncogene ( c foc , c jun , c mas ) gene transcripts in brain of 2 4 weeks old rats well correlated both with brain maturation in normal animals and development of brain weight deficiency in the irradiated rats . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NAP 22 , a neuronal tissue enriched acidic membrane protein , is a Ca ( 2+ ) dependent calmodulin binding protein and has similar biochemical characteristics to GAP 43 ( neuromodulin ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Apo calmodulin binds typical target sequences from skeletal muscle myosin light chain kinase and neuromodulin with Kd approximately 70 90 nM ( at low ionic strength ) . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
N terminal specific anti B 50 ( GAP 43 ) antibodies inhibit Ca ( 2+ ) induced noradrenaline release , B 50 phosphorylation and dephosphorylation , and calmodulin binding . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Calmodulin stabilizes an amphiphilic alpha helix within RC3 / neurogranin and GAP 43 / neuromodulin only when Ca2+ is absent . ^^^ Two neuronal protein kinase C substrates , RC3 / neurogranin and GAP 43 / neuromodulin , preferentially bind to calmodulin ( CaM ) when Ca2+ is absent . ^^^ CaM and GAP 43 . ^^^ CaM interactions by circular dichroism spectroscopy using purified , recombinant RC 3 and GAP 43 , sequence variants of RC 3 displaying qualitative and quantitative differences in CaM binding affinities , and overlapping peptides that cumulatively span the entire amino acid sequence of RC 3 . ^^^ We conclude that CaM stabilizes a basic , amphiphilic alpha helix within RC 3 and GAP 43 under physiological salt concentrations only when Ca2+ is absent . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The region of homology encompasses the calmodulin binding domain and protein kinase C ( PKC ) phosphorylation site of GAP 43 . ^^^ The fly proteins are shown to bind Drosophila calmodulin ( CaM ) , and are phosphorylated by purified PKC after a fashion predicted from prior work with vertebrate GAP 43 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Isolated GAP 43 can bind to actin and to calmodulin , and can activate the heterotrimeric GTP binding proteins , G ( o ) and Gi . ^^^ A peptide consisting of the GAP 43 sequence 39 55 binds calmodulin , and an amino terminal GAP 43 ( 1 10 ) peptide activates G ( o ) , suggesting that these stretches may be functional domains of the intact protein . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The role of several biological molecules in learning and memory are considered , for example , protein kinase C ( PKC ) , Ca ( ++ ) Calmodulin kinase 2 ( CaMKII ) , GAP 43 , and glutamate receptors . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Hence , consideration is given to several plausible roles for B 50 ( GAP 43 ) in vivo , which are discussed in the context of the cellular localization of the protein , significant posttranslational enzymes , and regulatory proteins , including protein kinases , phosphoinositides , calmodulin , and proteases . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Evidence for the binding of calmodulin to endogenous B 50 ( GAP 43 ) in native synaptosomal plasma membranes . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The results suggest that the biological roles of GAP 43 may depend on an ability to form a dynamic membrane cytoskeleton calmodulin complex . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
CaM complex coexist when Ca2+ is absent and that GAP 43 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Although it has been suggested that cytosolic calmodulin is increased by phosphorylation of the protein kinase C substrates , GAP 43 and MARCKS , we found no change in calmodulin levels by phorbol ester or beta bungarotoxin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Calmodulin ( CaM ) at > 5 microM inhibited phosphorylation , consistent with the presence of CaM binding activity at the site on F1 / GAP 43 acted upon by PKC . 7 . ^^^ Calmodulin ( CaM ) at > 5 microM inhibited phosphorylation , consistent with the presence of CaM binding activity at the site on F1 / GAP 43 acted upon by PKC . 7 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Calmodulin and de phosphorylated B 50 / growth associated protein 43 ( GAP 43 ) have been shown to bind in vitro in a molecular complex , but evidence for an in situ association in the nervous system does not exist . ^^^ To explore a putative function of B 50 / GAP 43 , namely , the capacity of binding calmodulin to the plasma membrane , we examined the ultrastructural distribution of calmodulin in the proximal unmyelinated axon shafts of this model , using double immunolabelling and detection by fluorescent or gold probes conjugated to second antibodies . ^^^ Immunofluorescence showed that seven days post sciatic nerve crush the calmodulin immunoreactivity , similar to B 50 / GAP 43 immunoreactivity , was intense in unmyelinated axon shafts located proximal to the site of injury of the regenerating nerve . ^^^ Over 60 % of the plasma membrane associated calmodulin co localized with B 50 / GAP 43 in a non random distribution . ^^^ Since normally calmodulin is largely present in the cytoplasm , these data suggest that calmodulin has been concentrated at the plasma membrane of unmyelinated axons , most probably by B 50 / GAP 43 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
GAP 43 also interacted with synaptotagmin and calmodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Xenopus laevis GAP 43 ( XGAP 43 ) is highly related to other vertebrate GAP 43 proteins in its N terminal region which contains a membrane targeting sequence , serine phosphorylation site , and calmodulin binding domain . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The nervous tissue specific protein B 50 ( GAP 43 ) , which has been implicated in the regulation of neurotransmitter release , is a member of a family of atypical calmodulin binding proteins . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
To investigate the molecular basis for GAP 43 function in axon outgrowth , we produced a mutant , GAP 43 ( Ala 41 ) , whose interaction with calmodulin in vitro was unaffected by increasing Ca2+ concentrations , and stably transfected it into GAP 43 deficient PC12B cells . ^^^ The phenotypic abnormalities resemble other cell types in which membrane skeleton / plasma membrane interactions have been functionally decoupled , and our results are consistent with the notion that these interactions may be abnormal in GAP 43 ( Ala 41 ) expressing PC12B cells , either as a direct consequence of the mutation or arising secondarily to the altered availability of calmodulin in the growing neurite . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
In contrast , unphosphorylated GAP 43 , which binds calmodulin , is always found in parts of the growth cone that are retracting . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Simulation of the interactions between the calpacitins CaM and Ca2+ imply that GAP 43 and RC 3 tune and homeostatically constrain the Ca2+ signal transduction system . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
GAP 43 is an abundant intracellular growth cone protein that can serve as a PKC substrate and regulate calmodulin availability . ^^^ Instead , GAP 43 appears to mediate RGC axon interaction with guidance cues in the lateral diencephalic wall , suggesting possible involvement of PKC and calmodulin signaling during optic tract formation . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
We have used in situ hybridization to study the expression of mRNAs for L 1 and its close homologue CHL 1 , by neurons regenerating their axons in vivo , and have compared CAM expression with that of GAP 43 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
We propose a model wherein RC 3 and GAP 43 regulate calmodulin availability in dendritic spines and axons , respectively , and calmodulin regulates their ability to amplify the mobilization of Ca2+ in response to metabotropic glutamate receptor stimulation . ^^^ The capacitance of the system is regulated by phosphorylation by protein kinase C , which abrogates interactions between calmodulin and RC 3 or GAP 43 . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
This region is not required for activation of isolated Go but is necessary for GAP 43 binding to isolated calmodulin and to isolated protein kinase C . ^^^ This mutation blocks GAP 43 binding to both protein kinase C and calmodulin . ^^^ Thus , GAP 43 regulates an oocyte signaling cascade via coordinated , simultaneous G protein activation and interaction with either calmodulin or protein kinase C . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Calmodulin , which binds to GAP 43 and inhibits its phosphorylation by protein kinase C , abolished the effect of TPA . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
GAP 43 is bound by calmodulin when Ca2+ levels are low , and releases the calmodulin when Ca2+ levels rise , suggesting that calmodulin may act as a negative regulator of GAP 43 during periods of low activity in the neurons . ^^^ To identify the function of GAP 43 during activity dependent increases in Ca2+ levels , when it is not bound to calmodulin , we sought proteins with which GAP 43 interacts in the presence of Ca2+ . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
This resemblance and the fact that GAP 43 also has been proposed to regulate calmodulin availability raise the possibility that calmodulin function is involved in CNS midline axon guidance in both vertebrates and invertebrates . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The protein kinase C ( PKC ) substrate GAP 43 is already expressed in neural precursor cells , colocalizes with PKCeta and binds calmodulin . ^^^ Phosphorylation of GAP 43 caused a disruption of its complex with calmodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The cleavage occurs in the region responsible for the interaction of GAP 43 with calmodulin . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Coimmunoprecipitation of specific components of CAM signaling pathways by GAP 43 then identified distinct subpopulations of DRMs . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
Administration of palmitoylcarnitine , although did not change the subcellular distribution of GAP 43 , decreased its phosphorylation , which could regulate other signal transduction pathways ( calmodulin and G ( 0 ) dependent ) . . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
In addition , calmodulin binding to GAP 43 decreases the rate of calpain mediated GAP 43 proteolysis . ^^^ Our results indicate that m calpain mediated GAP 43 proteolysis regulated by PKC and calmodulin is of physiological relevance , particularly in axonal growth cone guidance . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
The concentration of calmodulin in neurons is considerably less than the total concentration of the apocalmodulin binding proteins neurogranin and GAP 43 , resulting in a low level of free calmodulin in the resting state . ^^^ |
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Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P17677 and P62158 |
Pubmed |
SVM Score :0.0 |
NA |
|