| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| The vectors pDK 1 and pDK 2 provide unique sites for cloning selectable markers in Bacteroides . pOA 10 is a cosmid vector containing the replication region of pCP 1 necessary for maintenance in Bacteroides . pDK 3 , pDK4 . 1 , and pDK4 . 2 contain the Bacteroides clindamycin resistance gene allowing selection and maintenance in B . fragilis of plasmids containing inserted DNA fragments . pDK 3 was used to test the expression in B . fragilis of five foreign tetracycline resistance ( TcR ) genes . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Two subclones were isolated , designated pDK 1 and pDK 2 ; the former complemented the partial defect in the utilization of aspartate , although its exact function was not established . pDK 2 encoded the asparaginase 1 gene ( ansA ) , the coding region of which was further defined within a 1 . 7 kilobase fragment . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Recent evidence from this laboratory indicates that at least two isoenzymic forms of pyruvate dehydrogenase kinase ( PDK 1 and PDK 2 ) may be involved in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase complex by phosphorylation ( Popov , K . ^^^ In terms of their primary structures , two isoenzymes identified in humans correspond to rat PDK 1 and PDK 2 , whereas a third gene ( PDK 3 ) encodes for a new isoenzyme that shares 68 % and 67 % of amino acid identities with PDK 1 and PDK 2 , respectively . ^^^ The tissue distribution of PDK 1 mRNA differs markedly from PDK 2 . ^^^ In contrast to PDk 1 and PDK 2 , which are expressed in all tissues tested , the message for PDK 3 was found almost exclusively in heart and skeletal muscle , indicating that PDK 3 may serve specialized functions characteristic of muscle tissues . ^^^ In all tissues tested thus far , the level of expression of PDK 2 mRNA was essentially higher than that of PDK 1 and PDK 3 , consistent with the idea that PDK 2 is a major isoenzyme responsible for regulation of pyruvate dehydrogenase in human tissues . . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Tissue distribution and kinetic parameters for the four isoenzymes of pyruvate dehydrogenase kinase ( PDK 1 , PDK 2 , PDK 3 and PDK 4 ) identified thus far in mammals were analysed . ^^^ NADH alone stimulated the activities of PDK 1 and PDK 2 by 20 and 30 % respectively . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| In contrast with the findings for PDK 4 , little or no changes in the amounts of PDK 1 and PDK 2 protein and the abundance of their messages occurred in response to starvation and diabetes . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| The maize cDNAs are 1332 ( PDK 1 ) and 1602 ( PDK 2 ) nucleotides in length , encoding polypeptides with calculated molecular masses of 38 , 867 and 41 , 327 Da that share 77 % amino acid identity . ^^^ PDK 1 and PDK 2 were expressed in Escherichia coli with N terminal His 6 tags to facilitate purification . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| The serine threonine kinase Akt is a downstream target of phosphoinositide 3 kinase ( PI 3 kinase ) ; it is activated by the phosphoinositide 3 phosphate dependent kinases PDK 1 and PDK 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Activation of serum and glucocorticoid regulated protein kinase by agonists that activate phosphatidylinositide 3 kinase is mediated by 3 phosphoinositide dependent protein kinase 1 ( PDK 1 ) and PDK 2 . ^^^ The PtdIns ( 3 , 4 , 5 ) P 3 dependent activation of protein kinase B ( PKB ) by 3 phosphoinositide dependent protein kinases 1 and 2 ( PDK 1 and PDK 2 respectively ) is a key event in mediating the effects of signals that activate PtdIns 3 kinase . ^^^ The catalytic domain of serum and glucocorticoid regulated protein kinase ( SGK ) is 54 % identical with that of PKB and , although lacking the PtdIns ( 3 , 4 , 5 ) P 3 binding pleckstrin homology domain , SGK retains the residues that are phosphorylated by PDK 1 and PDK 2 , which are Thr 256 and Ser 422 in SGK . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| PDK 1 acquires PDK 2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK 2 . ^^^ Thr 308 is phosphorylated by the 3 phosphoinositide dependent protein kinase 1 ( PDK 1 ) but the identity of the kinase that phosphorylates Ser 473 ( provisionally termed PDK 2 ) is unknown . ^^^ Mutation of any of the conserved residues in the PDK 2 motif of PIF prevented interaction of PIF with PDK 1 . ^^^ Remarkably , interaction of PDK 1 with PIF , or with a synthetic peptide encompassing the PDK 2 consensus sequence of PIF , converted PDK 1 from an enzyme that could phosphorylate only Thr 308 of PKBalpha to one that phosphorylates both Thr 308 and Ser 473 of PKBalpha in a manner dependent on phosphatidylinositol ( 3 , 4 , 5 ) trisphosphate ( PtdIns ( 3 , 4 , 5 ) P 3 ) . ^^^ CONCLUSIONS : PDK 1 and PDK 2 might be the same enzyme , the substrate specificity and activity of PDK 1 being regulated through its interaction with another protein ( s ) . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Thr 308 is phosphorylated by the phosphoinositide dependent kinase 1 , ( PDK 1 ) , whereas the mechanism of phosphorylation of the hydrophobic site , tentatively referred to as the PDK 2 site , is unknown . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Here we report that the major PKB subtype in platelets is PKBalpha , which is activated by phosphorylation of Thr ( 308 ) and Ser ( 473 ) and has a constitutively phosphorylated Thr ( 450 ) that does not contribute to PKB activation . alpha Thrombin and thrombopoietin activate PKBalpha via PI 3K and trigger the concurrent phosphorylation of Thr ( 308 ) ( via PDK 1 ) and Ser ( 473 ) ( via a not yet identified PDK 2 ) . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Some of the inhibitor classes tested inhibited autophosphorylation of recombinant PDK 1 and PDK 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Akt activation requires phosphorylation of Thr ( 308 ) and Ser ( 473 ) by 3 phosphoinositide dependent kinase 1 and 2 ( PDK 1 and PDK 2 ) , respectively . ^^^ While PDK 1 has been cloned and sequenced , PDK 2 has yet to be identified . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| PDK 1 and 2 protein and mRNA were generally unaltered by fasting in all fiber types , except for increased PDK 2 mRNA in the fast oxidative fibers . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Aging decreased the levels of mRNAs for PDK 1 and 2 in cerebellum and increased the PDK 2 mRNA in hippocampus and cerebral cortex . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Here we report that the four isoenzymes of protein kinase responsible for the phosphorylation and inactivation of pyruvate dehydrogenase ( PDK 1 , PDK 2 , PDK 3 and PDK 4 ) differ in their abilities to phosphorylate the enzyme . ^^^ PDK 1 can phosphorylate all three sites , whereas PDK 2 , PDK 3 and PDK 4 each phosphorylate only site 1 and site 2 . ^^^ As a result , the amount of phosphate incorporated by each isoenzyme decreases in the order PDK 1 > PDK 3 > or=PDK4 > PDK 2 . ^^^ Secondly , thiamin pyrophosphate markedly decreases the amount of phosphate that PDK 1 incorporates in sites 2 and 3 and that PDK 2 incorporates in site 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| All four PDKs phosphorylated site 1 and site 2 , however , with different rates in phosphate buffer ( for site 1 , PDK 2 > PDK 4 approximately PDK 1 > PDK 3 ; for site 2 , PDK 3 > PDK 4 > PDK 2 > PDK 1 ) . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| We conclude that , at physiological concentrations , TNF alpha activates endogenous PKB by stimulating PDK 2 ( increase in Ser ( 473 ) phosphorylation ) in a PI 3 kinase dependent ( wortmannin sensitive ) manner , without causing detectable stimulation of PDK 1 ( no increase in Thr ( 308 ) phosphorylation ) or ARNO translocation . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Both R234Q and R234G mutant proteins displayed similar phosphorylation rates of sites 1 and 2 by pyruvate dehydrogenase kinase 2 ( PDK 2 ) and site 3 by PDK 1 compared to wild type E 1 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| In this study , using antibodies against PDK 1 , PDK 2 , and PDK 4 ( no sufficiently specific antibodies are as yet available for PDK 3 ) , we identified the PDK isoform profile of the pancreatic islet and delineated the effects of starvation ( 48 h ) on protein expression of individual PDK isoforms . ^^^ Rat islets were demonstrated to contain all three PDK isoforms , PDK 1 , PDK 2 , and PDK 4 . ^^^ Protein expression of PDK 1 and PDK 2 was suppressed in response to starvation ( by 27 % [ P < 0 . 01 ] and 10 % [ NS ] , respectively ) . ^^^ We demonstrated that activation of peroxisome proliferator activated receptor alpha ( PPAR alpha ) by the selective agonist WY 14 , 643 for 24 h in vivo leads to specific upregulation of islet PDK 4 protein expression by 1 . 8 fold ( P < 0 . 01 ) , in the absence of change in islet PDK 1 and PDK 2 protein expression but in conjunction with a 2 . 2 fold increase ( P < 0 . 01 ) in islet PPAR alpha protein expression . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Binding of PDK 1 and PDK 2 was readily reversible with the apparent dissociation constant of approx . 10 microM for both isoenzymes . ^^^ Monomeric L 2 domain alone had very little effect on the activities of either PDK 1 or PDK 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| PDK 1 has clearly been shown to phosphorylate the threonine , but the mechanism leading to phosphorylation of the serine , the PDK 2 site , is unclear . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| PDK 1 , an upstream effector of Akt , was also down regulated following CEES exposure , but two other upstream effectors of Akt , PI 3 K and PDK 2 , remained unchanged . 4 . ^^^ The phosphorylation of Akt at Ser ( 473 ) and Thr ( 308 ) was significantly decreased following CEES treatment , reflecting the suppressed kinase activity of both PDK 1 and PDK 2 . 5 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| PDK 2 and PDK 4 appear to be expressed in most major tissues and organs of the body , PDK 1 appears to be limited to the heart and pancreatic islets , and PDK 3 is limited to the kidney , brain and testis . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| R lipoic acid , S lipoic acid and R dihydrolipoic acid did not significantly affect activities of PDPs and at the same time inhibited PDKs to different extents ( PDK 1 > PDK 4 approximately PDK 2 > PDK 3 for R LA ) . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| In mammals , there are four genetically and biochemically distinct forms of PDK that are expressed in a tissue specific manner ( PDK 1 , PDK 2 , PDK 3 , and PDK 4 ) . ^^^ Here , we demonstrate that two members of the PDK family , PDK 1 and PDK 2 , form heterodimeric species when coexpressed in the same Escherichia coli cell . ^^^ The heterodimeric kinase was catalytically active and was clearly distinct from homodimeric PDK 1 or PDK 2 with respect to kinetic parameters , site specificity and regulation . ^^^ These data strongly suggest that heterodimerization between PDK 1 and PDK 2 adds another level of diversity to this protein family in addition to that which arises from gene multiplicity . . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Immunodepleting cytosolic PDK 1 from an in vitro reaction containing plasma membrane and cytosol markedly inhibited insulin stimulated phosphorylation of Akt at the PDK 1 site ( Thr 308 ) but had no effect on phosphorylation at the PDK 2 site ( Ser 473 ) . ^^^ Our data indicate that this PDK 2 activity is the result of a kinase distinct from PDK 1 and is not due to autophosphorylation or transphosphorylation of Akt . . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Akt interacts with these phospholipids , causing its translocation to the inner membrane , where it is phosphorylated and activated by PDK 1 and PDK 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| The unphosphorylated form of Akt 1 is virtually inactive and its full activation requires two phosphatidylinositol 3 , 4 , 5 triphosphate dependent phosphorylation events , Thr 308 by 3 phosphoinositide dependent kinase 1 ( PDK 1 ) and Ser 473 by an undefined kinase that has been termed PDK 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Membrane bound Akt is then phosphorylated at two sites for its full activation ; Thr 308 in the activation loop of the kinase domain is phosphorylated by 3 phosphoinositide dependent kinase 1 ( PDK 1 ) and Ser 473 in the C terminal hydrophobic motif by a putative kinase PDK 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Differential roles of PDK 1 and PDK 2 phosphorylation sites in the yeast AGC kinases Ypk 1 , Pkc 1 and Sch 9 . ^^^ Here , genetic and biochemical methods have been used to investigate the physiological consequences of phosphorylation at the PDK 1 and PDK 2 sites of Ypk 1 , Pkc 1 and Sch 9 . ^^^ It was found that phosphorylation at the PDK 1 site in the activation loop is indispensable for the essential functions of all three kinases in vivo , whereas phosphorylation at the PDK 2 motif plays a non essential and much more subtle role in modulating the ability of these kinases to regulate the downstream processes in which they participate . . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Here we show in starfish oocytes that when PDK 1 activity is inhibited by a neutralizing antibody , maturation inducing hormone fails to induce cyclin B Cdc 2 activation at the meiotic G 2 M phase transition , even though PDK 2 activity becomes detectable . ^^^ They further support that PDK 2 is a molecule distinct from PDK 1 and Akt , and that PDK 2 activity is not sufficient for the full activation of Akt in the absence of PDK 1 activity . . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| In addition to two known plasmids ( 380 kb pDK 1 and 330 kb pDK 2 ) , a third megaplasmid ( 750 kb pDK 3 ) was newly identified in DK 17 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| We also show that the carboxyl tails derived from isozymes PDK 1 , PDK 3 , and PDK 4 are capable of supporting the kinase activity of the kinase core derived from PDK 2 as well as binding of the respective PDK 2 chimeras to the lipoyl bearing domain . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| In contrast , the differences for PDH 2 were indicated as follows : ( 1 ) by a 2 . 4 fold increase in binding affinity for the PDH binding domain of dihydrolipoamide acetyltransferase as measured by surface plasmon resonance ; ( 2 ) by possible involvement of Ser 264 ( site 1 ) of PDH 2 in catalysis as evident by its kinetic behavior ; and ( 3 ) by the lower activities of PDK 1 , PDK 2 , and PDK 4 as well as PDP 1 and PDP 2 toward PDH 2 . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| Palmitate up regulated mRNA expression of PDK 1 ( 2 . 9 fold ) , PDK 2 ( 1 . 9 fold ) , and PDK 4 ( 3 . 1 fold ) . ^^^ High glucose increased PDK 1 ( 1 . 8 fold ) and PDK 2 ( 2 . 7 fold ) mRNA expression but reduced PDK 4 mRNA expression by 40 percent in cultured islets . ^^^ |
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| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q15118 and Q15119 |
Pubmed |
SVM Score :0.0 |
| NA |
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