| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.60749541 |
| Cotransfection of gamma PAK with constitutively active Cdc 42 induces gamma PAK activation and translocation , whereas inactive Cdc 42 inhibits both processes in response to hyperosmotic stress , suggesting that Cdc 42 has a role in the translocation and activation of gamma PAK . alpha PAK is not activated in response to hyperosmolarity in 3T3 L 1 cells . 0.60749541^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :1.0488748 |
| In 293T cells , WT Pak 2 , S141A , and S141D formed a stable complex with the constitutively active mutant Cdc 42 L61 , but not with the dominant negative Cdc 42 N17 . 1.0488748^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| After autophosphorylation of gamma PAK in the presence of Cdc 42 ( GTPgammaS ) or histone 4 , both cleavage products contain phosphate and gamma PAK is catalytically active . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| To examine the requirements for activation of the p 21 activated protein kinase gamma PAK ( Pak 2 , PAK 1 ) from rabbit reticulocytes by Cdc 42 ( GTPgammaS ) , autophosphorylation with ATP ( Mg ) or ATP ( Mn ) and its effects on protein kinase activity were examined . ^^^ However , gamma PAK autophosphorylated with ATP ( Mn ) in the presence or absence of Cdc 42 ( GTPgammaS ) did not phosphorylate peptide or protein substrates in the presence of ATP ( Mn ) , indicating that gamma PAK can utilize ATP ( Mn ) for autophosphorylation but not for phosphorylation of exogenous substrates . ^^^ Tryptic phosphopeptide maps of gamma PAK autophosphorylated with ATP ( Mg ) alone showed 3 phosphopeptides , while with Cdc 42 ( GTPgammaS ) a total of 9 major phosphopeptides was observed . ^^^ When gamma PAK was autophosphorylated with ATP ( Mn ) in the presence or absence of Cdc 42 ( GTPgammaS ) , 7 major phosphopeptides were observed , which were identical to peptides obtained with Cdc 42 ( GTPgammaS ) and ATP ( Mg ) . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| In this study we report that gamma PAK , which is activated by the GTP binding proteins Cdc 42 and Rac , catalyses phosphorylation of intact non muscle myosin 2 and isolated recombinant RLC . gamma PAK phosphorylated endothelial cell myosin 2 to 0 . 85 + / 0 . 02 mol PO 4 per mol RLC . ^^^ Endothelial cell monolayers permeabilized with saponin retract upon exposure to either Cdc 42 or trypsin activated gamma PAK and ATP . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Multisite autophosphorylation of p 21 activated protein kinase gamma PAK as a function of activation . p 21 activated protein kinase ( PAK ) is a family of serine / threonine kinases whose activity is stimulated by binding to small G proteins such as Cdc 42 and subsequent autophosphorylation . ^^^ Following Cdc 42 stimulated autophosphorylation , the two dimensional profiles of native and recombinant gamma PAK were characterized by a similar acidic shift , suggesting a common response to Cdc 42 . ^^^ To understand the effect of differential phosphorylation on its activation status , gamma PAK autophosphorylation was conducted in the presence or absence of activators such as Cdc 42 and histone 2 AS , followed by tryptic digestion and comparative two dimensional phosphopeptide mapping . ^^^ Overall , eight autophosphorylation sites were identified in Cdc 42 activated gamma PAK , six of which are in common with those previously reported in alpha PAK , while Ser 19 and Ser 165 appear to be uniquely phosphorylated in the gamma form . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| The p 21 activated protein kinase gamma PAK from rabbit , expressed in insect cells , is activated following binding of Cdc 42 ( GTPgammaS ) . ^^^ Other substrates such as the Rous sarcoma virus protein NC are phosphorylated by gamma PAK following activation by Cdc 42 ( GTPgammaS ) , but are not phosphorylated by T402A . ^^^ The data suggest that some substrates can override the requirement for Cdc 42 ( GTPgammaS ) , by activating gamma PAK directly . . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| The small GTPase Cdc 42 , its inhibitory subunit Rho GDI , the adapter protein Nck , gamma p 21 activated protein kinase ( gamma Pak ) , and cofilin were found to undergo rapid association with the developing phagosomes in these cells . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Downregulated proteins include p 21 activated kinase 2 and its upstream GTPase Cdc 42 . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| The dissociation constants of the p 21 binding domains of PAK 1 , PAK 2 , and the RasGAP related domain of IQGAP 1 , which all cause significant reduction of the intrinsic rate of GTP hydrolysis upon binding to Rac 1 GTP , are found to be 0 . 71 , 0 . 26 , and 2 . 13 microM for Rac 1 GTP , compared with that determined for Cdc 42 GTP at 2 . 9 , 20 . 5 , and 0 . 39 microM , respectively , under similar conditions . ^^^ These results suggest that p50RhoGAP , p 190 , Bcr , and 3BP 1 are all capable of acting as a negative regulator for Rac 1 mediated signaling , and that , although PAK 1 and IQGAP 1 can couple tightly with both Rac 1 and Cdc 42 , PAK 2 is likely to be a specific effector for Rac 1 instead of Cdc42 . . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| We have characterized the interactions of a 22 residue CRIB peptide derived from human PAK 2 [ PAK 2 ( 71 92 ) ] with Cdc 42 using proton and heteronuclear NMR spectroscopy . ^^^ Interaction of the 22 residue peptide PAK 2 ( 71 92 ) with GTP gammaS loaded Cdc 42 causes resonance perturbations in the 1H 15N HSQC spectrum of Cdc 42 that are similar to those observed for a longer ( 46 amino acid ) CRIB containing protein fragment [ Guo , W . , et al . ( 1998 ) Biochemistry 37 , 14030 14037 ] . ^^^ Proton NMR studies of PAK 2 ( 71 92 ) demonstrate structuring of PAK 2 ( 71 92 ) in the presence of GTP gammaS loaded Cdc 42 , through the observation of many nonsequential transferred NOEs . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Regulation of Xenopus p 21 activated kinase ( 10 PAK 2 ) by Cdc 42 and maturation promoting factor controls Xenopus oocyte maturation . ^^^ We show that the small GTPase Cdc 42 is required for maintenance of active endogenous 10 PAK 2 in resting stage 6 oocytes , whereas Rac 1 is not involved in this regulation . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Activation of gamma PAK in human embryonic kidney 293T cells by cotransfection with constitutively active Cdc 42 induces activation of c Abl , resulting in increased phosphotyrosine levels . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Cdc 42 independent activation and translocation of the cytostatic p 21 activated protein kinase gamma PAK by sphingosine . ^^^ Sites autophosphorylated on gamma PAK in response to sphingosine are identical to those obtained with Cdc 42 ( GTP ) . ^^^ Thus , gamma PAK is activatable via a Cdc 42 independent mechanism , suggesting sphingosine has a role in gamma PAK activation under conditions of cell stress . . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Caspase activated PAK 2 is regulated by subcellular targeting and proteasomal degradation . p 21 activated protein kinases ( PAKs ) are a family of serine / threonine protein kinases that are activated by binding of the p 21 G proteins Cdc 42 or Rac . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| PAK 2 is activated by autophosphorylation upon binding of small G proteins such as Cdc 42 and Rac in the GTP bound state . ^^^ The results indicate that 1 ) in the presence of Cdc 42 , PAK 2 autophosphorylation is a bipartite mechanism , with the regulatory domain autophosphorylated at multiple residues , whereas activation coincides with autophosphorylation of the catalytic domain at Thr 402 ; 2 ) the autophosphorylation reactions in regulatory domain are either a nonlimiting step or not required for activation of enzyme ; 3 ) the autophosphorylation at site Thr 402 on the catalytic domain occurs by an intermolecular mechanism and is required for phosphorylation of exogenous substrates examined ; 4 ) binding of the exogenous protein / peptide substrates at the active site of PAK 2 has little or no effect on the autoactivation of PAK 2 , suggesting that multiple regions of PAK 2 are involved in the enzyme substrate recognition . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Furthermore , we show that TGF beta stimulated PAK 2 activity is regulated by Rac 1 and Cdc 42 and dominant negative PAK 2 or morpholino antisense oligonucleotides to PAK 2 prevent the morphological alteration observed following TGF beta addition . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| The constitutively active form of Cdc 42 increases the association of Pak 2 with Syk . ^^^ Pak 2 coexpressed with an inactive form of Cdc 42 or kinase inactive Pak 2 interacts to a lesser extent with Syk , suggesting that Pak 2 Syk association is enhanced by Pak 2 activation . ^^^ Pak 2 short interfering RNA suppresses sorbitol mediated activation of endogenous Syk and JNK , thus identifying a novel pathway for JNK activation by Cdc 42 . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Activation of full length PAK 2 by Rac or Cdc 42 stimulates cell survival and protects cells from cell death , whereas caspase activated PAK 2p34 induces a cell death response . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Cdc 42 GTPase and its effectors , p 21 activated kinases Pak 2 and Pak 1 , are not upstream elements controlling the basal level or the stress induced activation of Pmk 1 . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| A novel serine kinase activated by rac1 / CDC42Hs dependent autophosphorylation is related to PAK 65 and STE 20 . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Interestingly , unlike PAK 65 , HPK 1 does not contain the small GTPase Rac1 / Cdc42 binding domain and does not bind to either Rac 1 or Cdc 42 , suggesting that HPK 1 . activation is Rac1 / Cdc42 independent . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| Myosin phosphorylation by human cdc 42 dependent S6 / H4 kinase / gammaPAK from placenta and lymphoid cells . ^^^ In these studies , S6 / H4 kinase purified to homogeneity from human placenta was activated in vitro by cdc 42 GTP , or protease incubation and MgATP dependent autophosphorylation . ^^^ |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q13177 and P60953 |
Pubmed |
SVM Score :0.0 |
| NA |
|