| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.56964941 |
| The rat CAK beta has a homology with mouse FAK over their entire lengths except for the extreme N terminal 88 residues and shares 45 % overall sequence identity ( 60 % identical in the catalytic domain ) , which indicates that CAK beta is a protein structurally related to but different from FAK . 0.56964941^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Whereas FAK predominantly localizes at focal adhesions , CAK beta localizes at the perinuclear region in fibroblasts . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( PYK 2 ) are structurally related tyrosine kinases . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Hic 5 is also known to associate with focal adhesion kinase ( FAK ) or the related CAKbeta , and with vinculin . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Chromsomes and DNA replication of rat kangaroo cells ( PtK 2 ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Cell cycle analysis and stimulation of rat kangaroo cells ( PtK 2 ) after pulse labeling . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Centrosome behavior in motile HGF treated PtK 2 cells expressing GFP gamma tubulin . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Five PTK mRNAs ( fgr , hck , fak , jak 2 , and flk 1 ) increased expression across all three models of activation . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We demonstrate here that leupaxin associates with a second FAK family member , PYK 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In contrast to Lyn , PYK 2 , FAK , MAPK / ERK1 , SAPK / JNK , and Cdk 5 , only Fyn could phosphorylate alpha synuclein . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We have found that leupaxin in murine osteoclasts is associated with both PYK 2 and pp125FAK in the osteoclast . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Our data also indicate that the enhanced Pyk 2 level found in FAK / MEF plays no role in 5 Src induced anchorage independence . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Formation of complexes between p190RhoGAP , Fgr , and the FAK related protein Pyk 2 were also detected in murine macrophages . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| CADTK / PYK2 is most closely related to p 125 ( FAK ) and both enzymes are expressed in WB and GN 4 cells . ^^^ Angiotensin 2 , which only slightly increases p 125 ( FAK ) tyrosine phosphorylation in GN 4 cells , substantially increased CADTK tyrosine autophosphorylation and kinase activity . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We and others have recently cloned a non receptor , calcium dependent tyrosine kinase ( CADTK ; also known as PYK 2 , CAKbeta , and RAFTK ) that shares both overall domain structure and 45 % amino acid identity with p 125 ( FAK ) . ^^^ We have studied the signaling , activation , and potential function of these related enzymes in GN 4 rat liver epithelial cells that express CADTK and p 125 ( FAK ) at roughly similar levels . p 125 ( FAK ) is nearly fully tyrosine phosphorylated in resting GN 4 cells . ^^^ In this report we assessed the contribution of CADTK and p 125 ( FAK ) to tyrosine phosphorylation of focal contact proteins . ^^^ When CADTK and p 125 ( FAK ) were transiently overexpressed in 293 ( T ) cells , both enzymes associated with paxillin , but the avidity of CADTK appeared to be greater . ^^^ In summary , in GN 4 rat liver epithelial cells stimulation of CADTK was highly correlated with paxillin tyrosine phosphorylation ; in addition , CADTK but not p 125 ( FAK ) was complexed to paxillin at detectable levels . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In contrast , insulin had no effect on CADTK but stimulated the tyrosine phosphorylation of Cbl and the tyrosine dephosphorylation of pp 125 ( FAK ) and p 130 ( cas ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Freshly isolated human monocytes do not express p 125 ( FAK ) but upon adherence to substrata activate the highly related calcium dependent tyrosine kinase ( CADTK ) , also known as Pyk 2 , CAKbeta , RAFTK , and FAK 2 . ^^^ These data suggest that in a cell type that lacks p 125 ( FAK ) , CADTK plays an early role in post adherence signaling . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| PKC depletion did not alter Ang 2 dependent tyrosine phosphorylation or activity of p 125 ( FAK ) , CADTK , Fyn or Src , but PKC depletion or incubation with GF109203X resulted in Ang 2 dependent EGF receptor tyrosine phosphorylation . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Several of these proteins were identified and include protein tyrosine kinase 2 ( also known as CAKbeta , RAFTK , and CADTK ) , pp 125 focal adhesion tyrosine kinase , pp 130 Crk associated substrate , paxillin , and Cbl . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Tyrosine kinases activated by AngII include c Src , focal adhesion kinase ( FAK ) , Pyk 2 ( CADTK ) , Janus kinases ( JAK 2 and TYK 2 ) , and the receptor tyrosine kinases Ax 1 , epidermal growth factor , and platelet derived growth factor . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We compared CADTK regulation with that of the highly homologous focal adhesion tyrosine kinase ( FAK ) . ^^^ Interestingly , CADTK tyrosine phosphorylated FAK when both were transiently expressed , but FAK did not phosphorylate CADTK . ^^^ Biochemical experiments confirmed direct CADTK phosphorylation of FAK . ^^^ This phosphorylation utilized tyrosine residues other than Tyr 397 , Tyr 925 , or Tyr576 / Tyr577 , suggesting that new SH 2 binding sites might be created by CADTK dependent FAK phosphorylation . ^^^ Last , expression of the CADTK carboxyl terminus ( CRNK ) abolished CADTK but not FAK autophosphorylation . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Full length DFak 56 cDNA encodes a phosphoprotein of 140 kDa , which shares strong sequence similarity not only with mammalian p 125 ( FAK ) but also with the more recently described mammalian Pyk 2 ( also known as CAKbeta , RAFTK , FAK 2 , and CADTK ) FAK family member . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The focal adhesion PTK family consists of the focal adhesion kinase ( FAK ) and the RAFTK / Pyk2 kinase ( also known as CAK beta and CADTK ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Proline rich tyrosine kinase 2 ( Pyk 2 ) ( also known as RAFTK , CAKbeta or CADTK ) has been identified as a member of the focal adhesion kinase ( FAK ) family of protein tyrosine kinases and it has been suggested that the mode of Pyk 2 activation is distinct from that of FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Freshly isolated peripheral blood monocytes lack focal adhesion kinase ( p 125 ( FAK ) ) but activate a second member of this kinase family , calcium dependent tyrosine kinase ( CADTK ; also known as Pyk2 / CAKbeta / RAFTK / FAK2 ) , upon adhesion or stimulation with chemokines . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The focal adhesion kinase ( FAK ) and cell adhesion kinase beta ( CAKbeta , PYK 2 , CADTK , RAFTK ) are highly homologous FAK family members , yet clearly have unique roles in the cell . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Recently , we and others have identified a novel protein tyrosine kinase termed RAFTK , ( also known as Pyk 2 or Cak beta ) , which is related to FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Differential signaling by the focal adhesion kinase and cell adhesion kinase beta . pp 125 ( FAK ) and CAKbeta / Pyk2 / CadTK / RAFTK are related protein tyrosine kinases . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Recent evidence indicates that integrin ligation results in activation of focal adhesion kinase ( pp125FAK ) , the prototype of a new subfamily of nonreceptor protein tyrosine kinase ( PTK ) , including FAKB and the proline rich tyrosine kinase 2 ( PYK 2 ) , also termed cell adhesion kinase beta or related adhesion focal tyrosine kinase . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Cell adhesion kinase beta ( CAKbeta ) is a protein tyrosine kinase closely related to focal adhesion kinase ( FAK ) in structure . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In this regard , we observed that FAK / cells expressed cell adhesion kinase beta ( CAKbeta ) , a protein tyrosine kinase of the FAK subfamily . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We found that a focal adhesion kinase ( FAK ) related protein , cell adhesion kinase beta ( CAKbeta ) , was bound in vitro by the SH 3 domain of embryonal Fyn associated substrate ( Efs ) , a docking protein structurally related to p130Cas ( Cas ) and HEF 1 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) and cell adhesion kinase beta ( CAKbeta ) / PYK2 / CADTK / RAFTK are protein tyrosine kinases that can colocalize with , bind to , and induce tyrosine phosphorylation of p 130 ( CAS ) and paxillin . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Cell adhesion kinase beta ( CAKbeta , also known as Pyk2 / CadTK / RAFTK ) is the second member of the focal adhesion kinase ( FAK ) subfamily . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The sea urchin FAK is more closely related to FAK from other deuterostomes than from invertebrate protostomes or to cell adhesion kinase beta ( CAKbeta / Pyk2 / FAK2 ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Related adhesion focal tyrosine kinase ( RAFTK ) , also known as proline rich tyrosine kinase 2 and cellular adhesion kinase beta , has been recently cloned and characterized as a member of the focal adhesion kinase ( FAK ) subfamily . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Proline rich tyrosine kinase 2 ( PYK 2 ) , also known as cellular adhesion kinase beta ( CAKbeta ) and related adhesion focal tyrosine kinase , is a second member of the FAK subfamily and is activated by an increase in intracellular calcium levels , or treatment with TNFalpha and UV light . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Pertussis toxin insensitive G proteins , most likely from G alpha 12 class , cause the activation of several cytoplasmic protein tyrosine kinases [ Src , Pyk 2 ( proline rich tyrosine kinase 2 ) , and Fak ( focal adhesion kinase ) ] . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Furthermore , the interaction of the activated integrin LFA 1 with its ligand intercellular adhesion molecule 1 induced the activation of the cytoplasmic tyrosine kinases focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( PYK 2 ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Of a focal adhesion kinase ( FAK ) family of non receptor protein tyrosine kinases , HUVECs were found to express FAK , but scarcely proline rich tyrosine kinase 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Expression of focal adhesion kinase ( p 125 FAK ) and proline rich tyrosine kinase 2 ( PYK2 / CAKb ) in cerebral metastases , correlation with VEGF R , ecNOS 3 labelling and morphometric data . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal Adhesion Kinase ( FAK ) and Proline rich Tyrosine Kinase 2 ( PYK 2 ) are related in molecular structure , and may have some overlapping functions in signal transduction associated with cell substratum adhesion . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The FAK related kinase , proline rich tyrosine kinase 2 ( Pyk 2 ) , is expressed in FAK ( / ) cells , yet it exhibits a perinuclear distribution and does not functionally substitute for FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Here we show that acrylamide induces morphological changes and tyrosine phosphorylation of focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( Pyk 2 ) , a member of the FAK subfamily , in human differentiating neuroblastoma SH SY5Y cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In the present work , we investigated and compared the activation of two related tyrosine kinases expressed in platelets : the proline rich tyrosine kinase 2 ( Pyk 2 ) and the focal adhesion kinase ( FAK ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) and the related proline rich tyrosine kinase 2 ( PYK 2 ) are non receptor protein tyrosine kinases that transduce extracellular signals through the activation of Src family kinases and are highly enriched in neurones . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Upstream mediators of mitogen activated protein kinase ( MAP kinase ) activation include focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( pyk 2 ) which are both expressed by chondrocytes . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The proline rich tyrosine kinase 2 ( Pyk 2 ) and focal adhesion kinase ( FAK ) are cytoskeleton associated protein kinases participating in integrin dependent signaling . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Proline rich tyrosine kinase 2 ( PYK 2 ) is a member of the focal adhesion kinase ( FAK ) family of nonreceptor protein tyrosine kinases . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| AIMS : Expression analysis of the protein tyrosine kinases , focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( Pyk 2 ) in high grade osteosarcomas . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Besides coupling with heterotrimeric G proteins to activate phospholipase C beta ( PLC beta ) , AT1R also activates receptor tyrosine kinases ( PDGF R , EGF R and IGF R ) and non receptor tyrosine kinases ( Src , Fyn , Yes , proline rich tyrosine kinase 2 ( Pyk 2 ) , focal adhesion kinase ( FAK ) and JAK 2 ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) and its related kinase , proline rich tyrosine kinase 2 ( PYK 2 ) , are major kinases activated by cell extracellular matrix adhesion . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In the present study , treatment of chondrocytes with the 110 kDa FN f or an activating antibody to the alpha5beta1 integrin was found to increase tyrosine autophosphorylation ( Tyr 402 ) of the proline rich tyrosine kinase 2 ( PYK 2 ) without significant change in autophosphorylation ( Tyr 397 ) of focal adhesion kinase ( FAK ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Both SETA and AIP 1 interacted with focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( PYK 2 ) , and c Cbl interacted with PYK 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The alpha ( 4 ) paxillin association mediates trans regulation by enhancing the activation of tyrosine kinases , focal adhesion kinase ( FAK ) and / or proline rich tyrosine kinase 2 ( Pyk 2 ) , based on two lines of evidence . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The focal adhesion kinase ( FAK ) family kinases including FAK and proline rich tyrosine kinase 2 ( PYK 2 ) are major tyrosine kinases activated by integrin engagement . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| HGF induced the redistribution of focal adhesions , the activation of focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( Pyk 2 ) and their increased association with beta 1 and beta 3 integrins , and the production of pro matrix metalloproteinase 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| MSU induced functional signaling by specific protein kinases ( p 38 , Src , and the focal adhesion kinase [ FAK ] family members proline rich tyrosine kinase 2 [ Pyk 2 ] and FAK ) was also examined using selective pharmacologic inhibitors and transfection of kinase mutants . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The nonreceptor tyrosine kinases focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( Pyk 2 ) are activated by integrins , growth factors , and mechanical stimuli , suggesting a potentially important role in the integration of environmental stimuli . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Having no intrinsic kinase activity , integrins recruit intracellular kinases , such as the focal adhesion kinase ( FAK ) or the related proline rich tyrosine kinase 2 ( PYK 2 ) , to initiate signal transduction . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Despite this increase in integrin subunit expression , autophosphorylation of adhesion dependent kinases , focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( PYK 2 ) , is significantly reduced . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| IGF 1 increased tyrosine phosphorylation of the focal adhesion kinase ( FAK ) Pyk 2 ( calcium dependent proline rich tyrosine kinase 2 ) to a much greater extent than FAK , and increased association of Src with Pyk 2 but not FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In this report , we investigated the role of proline rich tyrosine kinase 2 ( Pyk 2 ) and FAK with regard to influencing glioma cell phenotypes . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) and proline rich tyrosine kinase 2 ( PYK 2 ) are two related non receptor tyrosine kinases highly expressed in brain . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Neuronal precursor cell expressed , developmentally down regulated gene ( Nedd ) 9 was recognized to be identical to Crk associated substrate lymphocyte type ( Cas L ) , a docking protein that associates with a variety of signaling molecules , such as focal adhesion kinase ( FAK ) , proline rich tyrosine kinase 2 ( Pyk 2 ) , and Crk . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| One component of P 110 was identified as the FAK ( focal adhesion kinase ) Pyk 2 ( proline rich tyrosine kinase 2 ) , which was phosphorylated in a beta 2 integrin and Src family kinase dependent manner . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Treatment of these cells with FAK siRNA substantially reduced FAK expression , but did not affect the expression of proline rich tyrosine kinase 2 ( Pyk 2 ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of focal adhesion kinase ( FAK ) on Ser 732 is induced by rho dependent kinase and is essential for proline rich tyrosine kinase 2 mediated phosphorylation of FAK on Tyr 407 in response to vascular endothelial growth factor . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Immunohistochemical analyses of autotaxin ( ATX ) , ephrin B 3 , B cell lymphoma w ( BCLW ) , and protein tyrosine kinase 2 beta showed them to be expressed in invasive glioma cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The RAFTK cDNA clone , encoding a polypeptide of 1009 amino acids , has closest homology ( 48 % identity , 65 % similarity ) to the focal adhesion kinase ( pp125FAK ) . ^^^ Comparison of the deduced amino acid sequences also indicates that RAFTK , like pp125FAK , lacks a transmembrane region , myristylation sites , and SH 2 and SH 3 domains . ^^^ In addition , like pp125FAK , RAFTK contains a kinase domain flanked by large N terminal ( 426 residues ) and C terminal ( 331 residues ) domains , and the C terminal region contains a predicted proline rich stretch of residues . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The RAFTK cDNA , which encodes a polypeptide of 1 , 009 amino acids , shares 65 % homology to the focal adhesion kinase ( FAK ) , including several consensus motifs . ^^^ Coexpression of RAFTK and FAK proteins in megakaryocytic cells and blood platelets was observed . ^^^ Using a specific antibody to RAFTK and the monoclonal antibody 2A7 to FAK , FAK and RAFTK could be distinguished antigenically . ^^^ Similar to FAK , dephosphorylation of RAFTK was observed when adherent transfected COS cells were detached . ^^^ These data suggest that RAFTK is a novel member of the FAK family , that it localizes to focal adhesion like structures in CMK megakaryocytic cells , that it participates in integrinmediated signaling pathways in megakaryocytes , and that it is able to associate with the tyrosine kinases Src and Fyn as well as the adaptor protein Grb 2 via SH 2 phosphotyrosine interactions . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The related adhesion focal tyrosine kinase ( RAFTK ) , also known as PYK 2 and CAKbeta , is a tyrosine kinase that is homologous to the focal adhesion kinase ( FAK ) p125FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The related adhesion focal tyrosine kinase ( RAFTK ) is a novel cytoplasmic tyrosine kinase and a member of the focal adhesion kinase ( FAK ) gene family . ^^^ These results demonstrate that RAFTK is tyrosine phosphorylated during an early phase of platelet activation by an integrin independent mechanism and is not dependent on platelet aggregation , suggesting different mechanisms of regulation for FAK and RAFTK phosphorylation during platelet activation . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| RAFTK , the second member of the focal adhesion kinase ( FAK ) family , is known to be activated in response to calcium flux in neuronal cells and integrin stimulation in megakaryocytes and B cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| ATP and / or UTP produced increases in tyrosine phosphorylation of multiple proteins , including p 42 MAP ( ERK 2 ) kinase , related adhesion focal tyrosine kinase ( RAFTK ) ( PYK 2 , CAKbeta ) , focal adhesion kinase ( FAK ) , Shc , and protein kinase Cdelta ( PKCdelta ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Urea and NaCl differentially regulate FAK and RAFTK / PYK2 in mIMCD 3 renal medullary cells . ^^^ Two cytosolic tyrosine kinases , focal adhesion kinase ( FAK ) and the newly described FAK homolog , related adhesion focal tyrosine kinase ( RAFTK , also called PYK 2 and CAKbeta ) , have been implicated in signaling to multiple mitogen activated protein kinase ( MAPK ) pathways . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Related adhesion focal tyrosine kinase ( RAFTK ) ( also known as PYK 2 ) is a cytoplasmic tyrosine kinase related to the focal adhesion kinase ( FAK ) p 125 ( FAK ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Related Adhesion Focal Tyrosine Kinase ( RAFTK ; also known as Pyk 2 ) , is a member of the Focal Adhesion Kinase ( FAK ) subfamily and is activated by TNF alpha , UV light and increases in intracellular calcium levels . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In this study , we have investigated the role of RAFTK , a cytoplasmic tyrosine kinase related to focal adhesion kinase ( FAK ) , in heregulin mediated signal transduction in breast cancer cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Characterization of the tyrosine kinases RAFTK / Pyk2 and FAK in nerve growth factor induced neuronal differentiation . ^^^ The related adhesion focal tyrosine kinase ( RAFTK ) , a member of the focal adhesion kinase ( FAK ) family and highly expressed in brain , is a key mediator of various extracellular signals that elevate intracellular Ca ( 2+ ) concentration . ^^^ We investigated RAFTK and FAK signaling upon nerve growth factor ( NGF ) stimulation of PC 12 cells . ^^^ NGF induced the tyrosine phosphorylation of RAFTK in a time and dose dependent manner , whereas no change in the tyrosine phosphorylation of FAK was observed . ^^^ Confocal microscopic analysis demonstrated that RAFTK translocated from the cytoplasm to potential neurite initiation sites at the cell periphery , where RAFTK co localized with paxillin and bundled actin in the early phase ( within 5 min ) of NGF stimulation , whereas FAK co localized with paxillin at `` point contacts , ' ' which are the primary cell adhesion sites in neuronal cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Inhibitors of phosphatidylinositol 3 kinase ( PI 3 kinase ) / Akt ( LY 294002 ) , tyrosine kinases ( Herbimycin A ) and the cytotoxic agent adriamycin induced apoptosis of REH cells . beta 1 integrin ligation induced activation of Akt , and tyrosine phosphorylation of RAFTK and FAK , but not SYK in REH cells . ^^^ This suggested that RAFTK and FAK activation might be linked to Akt activation . ^^^ RAFTK and Akt were activated but FAK was not . ^^^ Using fibroblasts from FAK / mice , which express high levels of RAFTK , fibronectin plating enhanced Akt activation . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Additionally , FAK and related adhesion focal tyrosine kinase ( RAFTK ) / Pyk2 kinases were tyrosine phosphorylated by VEGF and found to be important for focal adhesion sites . ^^^ Thus , these studies define a mechanism for the regulatory role of VEGF in focal adhesion complex assembly in HBMECs via activation of FAK and RAFTK / Pyk2 . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In this study , we have investigated the role of RAFTK ( also termed Pyk2 / CAK beta ) , a cytoplasmic tyrosine kinase related to focal adhesion kinase ( FAK ) , in heregulin mediated signal transduction in breast cancer cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Here we show that overexpression of CAKbeta or Fyn , but not FAK , enhanced the tyrosine phosphorylation of coexpressed Hic 5 in COS 7 cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In that case , we confirm work of others that survival signals are transduced by FAK , phosphatidylinositol 3 ' kinase ( PI 3 kinase ) , and Akt / protein kinase B ( PKB ) . ^^^ However , when serum is absent , PI 3 kinase and Akt / PKB are not involved in the fibronectin FAK JNK survival pathway documented herein . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Correspondingly , in the FAK antisense cDNA transfectant cells treated with lower doses of TNF alpha in presence of 10 microg . mL ( 1 ) Chx , the PKB level was lower , but in the FAK antisense cDNA transfectants treated with higher doses of TNF alpha in presence of 10 microg . mL ( 1 ) Chx , the PKB level was higher . ^^^ In response to TNF alpha alone , FAK antisense cDNA transfectants showed a decrease in the level of PKB . ^^^ However , in the case of TNF alpha cotreated with wortmannin , a specific inhibitor of phosphatidylinositol 3 kinase ( PtdIns3K ) , the FAK antisense cDNA transfectants produced significantly less amounts of PKB than the control . ^^^ It seemed that FAK could stimulate PKB levels through a pathway not involving PtdIns3K . ^^^ These results suggest that FAK can affect the sensitivity of SMMC 7721 cells to TNF alpha / Chx induced apoptosis in a biphasic manner by regulating PKB levels . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We hypothesized that hypoosmotic stress induced activation of PKB and AP 1 in HepG 2 cells is dependent on an intact actin cytoskeleton and subsequent FAK phosphorylation . ^^^ Western blots measured cytoplasmic phosphorylated or total FAK and PKB . ^^^ RESULTS : Exposure to hypoosmotic stress resulted in activation of the following signaling messengers in a sequential fashion : ( 1 ) phosphorylation of FAK occurred by 2 min , ( 2 ) phosphorylation of PKB occurred by 10 min , ( 3 ) nuclear translocation of AP 1 occurred by 30 min . ^^^ CONCLUSION : Actin reorganization following hypoosmotic stress is essential for the FAK mediated activation of the PI 3 K / PKB / AP 1 proliferative cascade . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The relationship between PTEN expression and anoikis in 8 different human lung carcinoma cell ( HLCC ) lines , and PKB and FAK effects in the process were studied . ^^^ Northern blots and Western blots were carried out to analyze PTEN expression at mRNA and protein levels and the phosphorylation level of PKB / FAK in HLCC lines , and anoikis was examined by using DNA Ladder analysis . ^^^ PTEN decreased the phosphorylation level of PKB and down regulated FAK expression in HLCC . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The decrease of protein kinase B ( PKB ) phosphorylation was present in this signaling pathway , but focal adhesion kinase ( FAK ) was not involved . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| This suppression was induced through downregulation of the Akt / PKB pathway , dephosphorylation of focal adhesion kinase ( FAK ) and mitogen activated protein kinase ( MAPK ) and cell cycle arrest at the G2 / M phase , but not the G 1 phase . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In this paper , we focus on the effects of TGF beta 1 on two important anti apoptotic protein kinases , protein kinase B ( PKB ) , and focal adhesion kinase ( FAK ) , in SMMC 7721 cells . ^^^ Furthermore , we also failed to detect PKB Ser 473 and FAK Tyr phosphorylation with various concentrations of TGF beta 1 treatment when cells were kept in suspension . ^^^ The above results indicate that PKB Ser 473 and FAK Tyr phosphorylation stimulated by TGF beta 1 are both dependent on cell adhesion . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| However , a possible role for ROS generation in mediating the ET 1 response on extracellular signal regulated kinases 1 and 2 ( ERK1 / 2 ) , protein kinase B ( PKB ) , and protein tyrosine kinase 2 ( Pyk 2 ) , key components of the growth promoting and proliferative signaling pathways , has not been examined in detail . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Caspase 8 activity was reduced in cells cultured on matrix , whereas focal adhesion kinase ( FAK ) , protein kinase B ( PKB , or Akt ) , and extracellular signal regulated kinase ( ERK ) phosphorylation was augmented . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Then we studied the changes of FAK , ILK , beta catenin , and PKB in this apoptotic model by Western blot . ^^^ RESULTS : We found that the loss or decrease of cell adhesion signal molecules is an important reason in apoptosis of SMMC 7721 hepatocellular carcinoma cell and the apoptosis of SMMC 7721 cell was preceded by the loss or decrease of FAK , ILK , PKB , and beta catenin or the damage of cell matrix and cell cell adhesion . ^^^ CONCLUSION : Our results suggested that the decrease of adhesion signal molecules , FAK , ILK , PKB , and beta catenin , could induce hepatocellular carcinoma cell apoptosis . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| A monoclonal antibody raised in vitro against the brain enzyme inhibits brain PTK as well as placental PTK 2 , but has no effect against PTK 1 or pp60src . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In this study we assayed autoantibodies to cytoskeletal cytoskeletal cytokeratin filaments , intermediate filaments of epithelial cells , by indirect immunofluorescence technique ( IIF ) using cultured human amnion epithelial cells and PtK 2 cells as targets . ^^^ Patients with ALD had a significantly increased prevalence of cytokeratin filament autoantibodies using both PtK 2 cells ( 69 % ) and human amnion epithelial cells ( 69 % ) as substrate , as compared to other groups . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Antibodies to 2 types of cytoplasmic intermediate filaments ( IMF ) vimentin and cytokeratin filaments were assayed in sera from various rheumatic diseases by indirect immunofluorescence using cultured human embryonic fibroblasts and an epithelial cell line , PtK 2 , as substrates . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Here we show that adhesion of murine NIH3T3 fibroblasts to fibronectin promotes SH 2 domain mediated association of the GRB 2 adaptor protein and the c Src protein tyrosine kinase ( PTK ) with FAK in vivo , and also results in activation of mitogen activated protein kinase ( MAPK ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Astral and spindle forces in PtK 2 cells during anaphase B : a laser microbeam study . ^^^ Rat kangaroo kidney epithelium ( PtK 2 ) cells develop prominent asters and spindles during anaphase B of mitosis . ^^^ To further test these inferences , we used a UV laser microbeam to damage one of the two asters in living PtK 2 cells at early anaphase B and monitored the effects on individual spindle pole movements , pole pole separation rates and astral microtubules ( MTs ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) is a nonreceptor protein tyrosine kinase ( PTK ) that associates with integrin receptors and participates in extracellular matrix mediated signal transduction events . ^^^ We showed previously that the c Src nonreceptor PTK and the Grb 2 SH2 / SH3 adaptor protein bound directly to FAK after fibronectin stimulation ( D . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( pp125FAK ) expression , activation and association with paxillin and p50CSK in human metastatic prostate carcinoma . pp125FAK , a protein tyrosine kinase ( PTK ) co localized with integrins in focal adhesion plaques , is known to transduce signals involved in the regulation of cell adhesion and motility as well as the anchorage independent growth of transformed cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The focal adhesion kinase ( FAK ) , a protein tyrosine kinase ( PTK ) , associates with integrin receptors and is activated by cell binding to extracellular matrix proteins , such as fibronectin ( FN ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| It has been demonstrated that ligation of VLA 4 induces phosphorylation of the protein tyrosine kinase ( PTK ) pp125FAK as well as other proteins which may be involved in the regulation of ligand affinity . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| FN stimulated c Src PTK activity was enhanced by wild type FAK expression , whereas FN stimulated activation of ERK 2 was blocked by expression of the c Src binding site Phe 397 mutant of FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Because the focal adhesion kinase pp125FAK plays a key role in adhesion / motility and is highly expressed in advanced PCa , we examined whether in PC 3 cells bombesin signal transduction triggers the tyrosine phosphorylation of this PTK and of associated integrins and signaling proteins likely to be present in focal adhesion plaques . pp125FAK tyrosine phosphorylation was stimulated by bombesin and mimicked by PKC activation with the tumor promotor phorbol 12 myristate 13 acetate ( PMA ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We presume that PTK activity , especially tyrosine phosphorylation of FAK , is decisively involved in the regulation of spontaneous T lymphocyte locomotion , which is independent of PKC activity . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Treatment of fibroblasts with protein kinase C inhibitors or with the PTK inhibitor herbimycin A or PP 1 resulted in reduced Src PTK activity , no Grb 2 binding to FAK , and lowered levels of ERK 2 activation . ^^^ FN stimulated FAK PTK activity was not significantly affected by herbimycin A treatment and , under these conditions , FAK autophosphorylation promoted Shc binding to FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Nuclear matrix lamina intermediate filament system in PtK 2 cells ] . ^^^ Selective extraction , whole mount cell preparation and DGD embeddment free section were involved in visualizing the nuclear matrix lamina intermediate filament system in PtK 2 cells . ^^^ Antibody to 280 kD nuclear matrix protein which were positive stained in HeLa cells could not react with the nuclear matrix components of PtK 2 cells . 2 D electrophoresis demonstrated that there were some differences in the composition of the nuclear matrix lamina intermediate filament system of HeLa and PtK 2 cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The focal adhesion kinase ( FAK ) protein tyrosine kinase ( PTK ) links transmembrane integrin receptors to intracellular signaling pathways . ^^^ We show that expression of the FAK related PTK , Pyk 2 , is elevated in fibroblasts isolated from murine fak / embryos ( FAK ) compared with cells from fak+ / + embryos ( FAK+ ) . ^^^ Significantly , repression of endogenous Src family PTK activity by p 50 ( csk ) overexpression inhibited FN stimulated cell spreading , Pyk 2 tyrosine phosphorylation , Grb 2 binding to Shc , and ERK 2 activation in the FAK but not in FAK+ cells . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| This review will focus on the functions of the focal adhesion kinase ( FAK ) protein tyrosine kinase ( PTK ) and its role in linking integrin receptors to intracellular signaling pathways . ^^^ Focus will be placed on the structural domains and sites of FAK tyrosine phosphorylation important for FAK mediated signaling events and how these sites are conserved in the FAK related PTK , Pyk 2 . ^^^ FAK re expression in the FAK cells confirms the role of this PTK in the regulation of cell morphology and in promoting cell migration events . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Emphasis is placed on the knowledge gained from studies using FAK null cells as a model system to decipher the role of this PTK in promoting cell motility . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The focal adhesion ( FAK ) non receptor protein tyrosine kinase ( PTK ) links both extracellular matrix / integrin and growth factor stimulation to intracellular signals promoting cell migration . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| One potential PTK that may regulate these signaling cascades is focal adhesion kinase ( FAK ) , a nonreceptor PTK associated with focal adhesions . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In contrast , disruption of cell substrate adhesion causes a decrease in FAK PTK activity that rapidly returns to control levels when the cells are plated on fibronection coated dishes . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Based on the genes studied , we could propose a general pathway for the cell reaction according to the surface treatments used : ( 1 ) metal ion release changes the time course of gene expression in the FAK pathway ; ( 2 ) once the accumulation of metal ions released from the Ti surface exceeds a threshold value , cell growth is diminished and apoptosis may be activated ; ( 3 ) PTK up regulation is also induced by metal ion release ; ( 4 ) the expression of Bcl 2 family and Bax may suggest that metal ions induce apoptosis . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The following describes an in situ / overlay technique in which purified PTK ( in our case , FAK ) can be used to identify potential substrates from filter lifts of protein produced from a cDNA expression library . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) , a member of a growing family of structurally distinct protein tyrosine kinases ( PTK ) , has been linked to specific phosphorylation events , and the elevation of FAK activity in human carcinoma cells correlated with increased invasive potential . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) is a 125 kDa protein tyrosine kinase ( PTK ) associated with focal adhesion in many cells , which plays a major role in the integrity of cytoskeletal structure . ^^^ FAK is a 125 kDa PTK associated with focal adhesion in many cells , and it plays a major role in the integrity of cytoskeletal structure . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We present a model for rapid control of CFTR and NKCC in chloride cells that includes : ( 1 ) activation of NKCC and CFTR via cAMP / PKA , ( 2 ) activation of NKCC by PKC , myosin light chain kinase ( MLCK ) , p 38 , OSR 1 and SPAK , ( 3 ) deactivation of NKCC by hypotonic cell swelling , Ca ( 2+ ) and an as yet unidentified protein phosphatase and ( 4 ) involvement of protein tyrosine kinase ( PTK ) acting on FAK to set levels of NKCC activity . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Focal adhesion kinase ( FAK ) , a member of a growing family of structurally distinct protein tyrosine kinases ( PTK ) , has been linked to specific phosphorylation events , and the elevation of FAK activity in human carcinoma cells is associated with increased invasive potential . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Queried by gene , the most frequently amplified kinase was PTK 2 ( 79 % of tumors ) , whereas the most frequently lost kinase was PTK2B ( hemizygous loss in 34 % of tumors ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Collectively , these findings indicate that activation of FAK and Src is dependent on actin cytoskeleton integrity , Rho activation , and adhesion to extracellular matrix , whereas ERK activation is independent of these intracellular events and seems to correlate with activation of the newly identified protein tyrosine kinase PYK 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| T cell receptor engagement induces tyrosine phosphorylation of FAK and Pyk 2 and their association with Lck . ^^^ Focal adhesion kinase ( FAK ) and the recently described Pyk 2 kinase are homologous members of a non receptor protein tyrosine kinase family . ^^^ In this study we show that FAK and Pyk 2 are two of the major 115 to 120 kDa proteins that become tyrosine phosphorylated in T cells following TCR complex stimulation . ^^^ The increase in tyrosine phosphorylation of both FAK and Pyk 2 , however , occurs in Lck deficient cells suggesting that phosphorylation of both of these kinases does not require Lck . ^^^ Taken together , these results suggest that FAK and Pyk 2 , perhaps in coordination with Lck , play a role in T cell activation . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Both pp 105 and pp 115 are antigenically distinct from HEF 1 , p130Cas , pp125FAK , Pyk 2 , p120cbl , and the p 110 subunit of phosphatidylinositol 3 kinase . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Differential regulation of Pyk 2 and focal adhesion kinase ( FAK ) . ^^^ Pyk 2 is a recently described cytoplasmic tyrosine kinase that is related to focal adhesion kinase ( FAK ) and can be activated by a variety of stimuli that elevate intracellular calcium . ^^^ In this report , we showed that Pyk 2 and FAK tyrosine phosphorylation are regulated differentially by integrin mediated cell adhesion and soluble factors both in rat aortic smooth muscle cells , which express endogenous Pyk 2 and FAK , and in transfected Chinese hamster ovary cells . ^^^ We also found that Pyk 2 is diffusely present throughout the cytoplasm , while FAK is localized in focal contacts as expected , suggesting that the different localization may account for their differential regulation . ^^^ By analyzing a chimeric protein contain N terminal and kinase domains of Pyk 2 and C terminal domain of FAK , we provided evidence that the distinctive C terminal domains of Pyk 2 and FAK were responsible for their differential regulation by integrins and soluble stimuli as well as their subcellular localization . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In this study , we show that in MC3T3 E 1 cells , fluoroaluminate induces a 110 kDa tyrosine phosphorylated protein that we identify as Pyk 2 , a cytoplasmic tyrosine kinase related to Fak ( focal adhesion kinase ) . ^^^ Although MC3T3 E 1 cells express much more Fak than Pyk 2 , Src preferentially associated with Pyk 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| As the same set of stimuli appear capable of stimulating FAK and / or PYK 2 in non neuronal cells and in cell lines with neuronal characteristics , we investigated the selectivity of regulation of these two kinases in mature nervous tissue . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| It is a multi domain adapter protein capable of interacting with several structural and signaling proteins including vinculin , FAK , PYK 2 , Src and Crk . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| CD 28 ligation induces tyrosine phosphorylation of Pyk 2 but not Fak in Jurkat T cells . ^^^ We examined whether the tyrosine kinases Pyk 2 and Fak ( members of the focal adhesion kinase family ) are involved in CD 28 signaling . ^^^ We found that ligating CD 28 in Jurkat T cells rapidly increases the tyrosine phosphorylation of Pyk 2 but not of Fak . ^^^ Paxillin , a substrate for Pyk 2 and Fak , was not tyrosine phosphorylated after CD 28 ligation . ^^^ These data provide evidence for the involvement of Pyk 2 in the CD 28 signaling cascade and suggest that neither Fak nor paxillin is involved in the signaling pathways of CD28 . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Blood platelets have recently been shown to express PYK 2 , a nonreceptor tyrosine kinase belonging to the FAK gene family . ^^^ Platelet intracellular Ca2+ mobilization induced by thrombin was hardly inhibited by these PKC inhibitors . p130Cas is a docking protein that associates with FAK or PYK 2 through the SH 3 domain . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Induced focal adhesion kinase ( FAK ) expression in FAK null cells enhances cell spreading and migration requiring both auto and activation loop phosphorylation sites and inhibits adhesion dependent tyrosine phosphorylation of Pyk 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The overall protein structure and deduced amino acid sequence of Dfak 56 show significant similarity to those of FAK and PYK 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Regulation of T cell receptor and CD 28 induced tyrosine phosphorylation of the focal adhesion tyrosine kinases Pyk 2 and Fak by protein kinase C . ^^^ The PTKs of the focal adhesion family , Pyk 2 and Fak , have been implicated in the signaling of TCR and CD 28 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We report the identification of a novel Pyk 2 interacting protein designated FIP 200 ( FAK family kinase interacting protein of 200 kD ) by using a yeast two hybrid screen . ^^^ In vitro binding assays and coimmunoprecipitation confirmed association of FIP 200 with Pyk 2 , and similar assays also showed FIP 200 binding to FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| HFS enhanced association of the src family kinases fyn and c src with an approximately 120 kDa tyrosine phosphorylated component containing the focal adhesion kinase ( FAK ) and its homologue PYK 2 . ^^^ Association of fyn with FAK and of c src with PYK 2 was increased following the HFS . ^^^ These results suggest that fyn and c src are involved in distinct signaling pathways and provide evidence for activation of FAK and PYK 2 following synaptic stimulation inducing LTP in vitro . . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Pyk 2 and FAK differentially regulate progression of the cell cycle . ^^^ In this report , we have analyzed the potential role and mechanism of Pyk 2 , a tyrosine kinase closely related to FAK , in cell cycle regulation by using tetracycline regulated expression system as well as chimeric molecules . ^^^ We have found that induction of Pyk 2 inhibited G ( 1 ) to S phase transition whereas comparable induction of FAK expression accelerated it . ^^^ Furthermore , expression of a chimeric protein containing Pyk 2 N terminal and kinase domain and FAK C terminal domain ( PFhy 1 ) increased cell cycle progression as FAK . ^^^ Conversely , the complementary chimeric molecule containing FAK N terminal and kinase domain and Pyk 2 C terminal domain ( FPhy 2 ) inhibited cell cycle progression to an even greater extent than Pyk 2 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Pyk 2 and FAK regulate neurite outgrowth induced by growth factors and integrins . ^^^ Pyk 2 and FAK associate with adhesion based complexes that contain epidermal growth factor ( EGF ) receptors , through their carboxy and amino terminal domains . ^^^ Expression of the C terminal domain of Pyk 2 or of FAK is sufficient to block neurite outgrowth , but not activation of extracellular signal regulated kinase ( ERK ) . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| These results indicate that CD 146 is coupled to a FYN dependent pathway that triggers Ca ( 2+ ) flux via phospholipase C gamma activation leading subsequently to the tyrosine phosphorylation of downstream targets such as Pyk 2 , p 130 ( Cas ) , FAK , and paxillin . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Pyk 2 is a member of the focal adhesion kinase ( FAK ) family , highly expressed in the central nervous system and haemopoietic cells . ^^^ Although Pyk 2 is homologous to FAK , its role in signaling pathways was shown to be distinct from that of FAK . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Several CD 2 pathway components regulated by p 59 ( fyn ) have been identified including phospholipase C gamma 1 ( PLC gamma 1 ) , Vav , protein kinase C theta isoform ( PKC theta ) , docking protein ( Dok ) , focal adhesion kinase ( FAK ) and Pyk 2 . ^^^ Furthermore , that FAK and Pyk 2 are target substrates implies that p 59 ( fyn ) may be an important regulator of T cell adhesion as well . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Proline rich tyrosine kinase 2 ( PYK 2 ) , a tyrosine kinase structurally related to focal adhesion kinase ( FAK ) , is implicated in regulating cytoskeletal organization . ^^^ Here we report identification of PSGAP , a novel protein that interacts with PYK 2 and FAK and contains multiple domains including a pleckstrin homology domain , a rhoGTPase activating protein domain , and a Src homology 3 domain . ^^^ Remarkably , PYK 2 , but not FAK , can activate CDC 42 via inhibition of PSGAP mediated GTP hydrolysis of CDC 42 . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Levels of the related protein , proline rich tyrosine kinase 2 ( Pyk 2 ) and the FAK substrate paxillin , were unaffected by the addition of oligonucleotides , whereas FAK expression was reduced by 70 % . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Two focal adhesion family kinases , Pyk 2 and , to a lesser extent , FAK were inducibly phosphorylated , as was a potential substrate , Cas . ^^^ |
|
| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Different modes and qualities of tyrosine phosphorylation of Fak and Pyk 2 during epithelial mesenchymal transdifferentiation and cell migration : analysis of specific phosphorylation events using site directed antibodies . ^^^ Here , we examined the regulation of Fak and Pyk 2 , kinases implicated in this phosphorylation . ^^^ During cell migration , these phosphorylation events , except Fak Tyr 397 , were augmented further , and phosphorylation of Fak Tyr 577 and the corresponding Pyk 2 Tyr 580 , both within the kinase activation loops , was also induced . ^^^ Although Fak and Pyk 2 have several phosphorylation sites in common , Tyr 407 and Tyr 861 are unique to Fak . ^^^ Our results revealed that Fak and Pyk 2 are non equivalent in the tyrosine phosphorylation events and thereby likely to evoke different downstream signaling cascades during EMT and cell migration of NMuMG cells . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The migration of FAK overexpressing cells directly correlated with the beta 1 integrin inducible tyrosine phosphorylation of endogenous plus wild type exogenous FAK , and not with phosphorylation of the FAK related kinase , Pyk 2 . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Cannabinoids increased phosphorylation of p 130 Cas , a protein associated with FAK , but had no effect on PYK 2 , a tyrosine kinase related to FAK and enriched in hippocampus . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| To identify the tyrosine phosphorylated proteins required for osmotic shock stimulated glucose uptake , we examined tyrosine phosphorylation of candidate proteins , and found that the 60 80kDa species including paxillin and the 120 130kDa species including p130Cas , PYK 2 , FAK and Gab 1 were tyrosine phosphorylated in response to osmotic shock . ^^^ Inhibition of actin polymerization by cytochalasin D significantly decreased the tyrosine phosphorylation of paxillin , p130Cas , PYK 2 and FAK but not Gab 1 , but had no effect on 2 deoxyglucose ( DOG ) uptake , suggesting a role for Gab 1 in osmotic shock induced glucose transport . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| GM CSF increased the expression of G protein coupled receptor kinase 3 ( GRK 3 ) , beta arrestin 1 , Pyk 2 , and focal adhesion kinase ( FAK ) . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| FAK regulates tyrosine phosphorylation of CAS , paxillin , and PYK 2 in cells expressing 5 Src , but is not a critical determinant of 5 Src transformation . ^^^ FAK was also shown to negatively regulate 5 Src mediated phosphorylation of the FAK related kinase PYK 2 . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Paxillin associates with numerous signaling molecules including adaptor molecules ( p130Cas , CRK ) , kinases ( FAK , Pyk 2 , PAK and SRC ) , tyrosine phosphatases ( PTP PEST ) , ARF GAP proteins ( p95pkl , PAG 3 ) and papillomavirus E 6 oncoproteins . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Some of these tyrosine phosphorylated bands were identified as the focal adhesion proteins paxillin , FAK , PYK 2 , and the c Met receptor itself . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Cas , Fak and Pyk 2 function in diverse signaling cascades to promote Yersinia uptake . ^^^ Using a reconstitution approach in Fak ( / ) fibroblasts , we have been able to specifically address the interplay between Fak , Cas and Pyk 2 in this process . ^^^ By contrast , Cas mediated uptake in the absence of Fak requires Crk as well as the protein tyrosine kinases Pyk 2 and Src . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| GFP FRNK overexpression suppressed basal and ET induced FAK phosphorylation and also inhibited ET induced phosphorylation of PYK 2 , the other member of the FAK family of nonreceptor protein tyrosine kinases . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Protein levels of protein tyrosine kinase 2 ( PYK 2 ) , activity regulated cytoskeletal protein ( ARC ) , as well as an antigen related to nerve growth factor 1 B ( NGFI B RA ) were shown to be significantly induced after cocaine administration . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In addition , Ang 2 activates many intracellular tyrosine kinases that play a role in growth signaling and inflammation , such as Src , Pyk 2 , p130Cas , FAK and JAK / STAT . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We therefore studied the effect of calcitonin on the tyrosine phosphorylation and subcellular distribution of paxillin , HEF 1 , FAK , and Pyk 2 , a FAK related tyrosine kinase , in osteoclasts . ^^^ Osteoclasts expressed both Pyk 2 and FAK , with Pyk 2 much more highly expressed . ^^^ Some of the punctate structures stained either for Pyk 2 alone or FAK alone . ^^^ Treatment with calcitonin disrupted the actin ring and induced the loss of the peripheral staining of paxillin , Pyk 2 , and FAK . ^^^ In calcitonin treated osteoclast like cells , the tyrosine phosphorylation of paxillin and FAK increased , whereas the tyrosine phosphorylation of Pyk 2 decreased . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| The magnitude of TyrP differed with the different FAK and PYK 2 sites . ^^^ These results demonstrate that CCK stimulates tyrosine phosphorylation of each of the three homologous phosphorylation sites in FAK and PYK 2 . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We investigated the role of the cytoplasmic tyrosine kinases FAK and Pyk 2 , potential integrin effectors , in the phenotypic determination of four different human glioblastoma cell lines . ^^^ Overexpression of Pyk 2 stimulated migration , whereas FAK overexpression inhibited cell migration and stimulated cellular proliferation . ^^^ These data suggest that FAK and Pyk 2 function as important signaling effectors in gliomas and indicate that their differential regulation may be determining factors in the temporal development of proliferative or migrational phenotypes . . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Prolin rich kinase 2 ( PYK 2 ) is a nonreceptor tyrosine kinase related to the focal adhesion kinase ( FAK ) p 125 ( FAK ) . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In the presence of PIAS 1 and SUMO 1 , FAK was sumoylated in intact cells , whereas PYK 2 , a closely related enzyme , was not . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| MCF 7ADR cells expressed higher levels of c Src , focal adhesion kinase ( FAK ) , and protein tyrosine kinase 2 ( PYK 2 ) involved in cell adhesion and motility . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Conversely , the FAK homologue proline rich tyrosine kinase 2 ( PYK 2 ) was found to be expressed both in normal and leukemic myeloid cells . ^^^ Moreover , FAK expression was correlated with the phosphorylation of PYK 2 on Tyr 881 , a critical site for the PYK 2 function in cell migration . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Differential regulation of FAK and PYK 2 tyrosine phosphorylation after electroconvulsive shock in the rat brain . ^^^ It has been suggested that FAK and PYK 2 have differential regulatory pathways and differential functions in the central nervous system . ^^^ In the present article , the authors examined the effect of ECS on PYK 2 and FAK mediated signaling in the rat cerebral cortex and hippocampus . ^^^ Our results showed that ECS activated PYK 2 more preferentially than FAK in both the cortex and the hippocampus . ^^^ The association of Src family kinases with FAK and PYK 2 was also distinctively affected by ECS ; Src was mainly associated with PYK 2 while Yes was associated with FAK . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Expression of tyrosine kinases FAK and Pyk 2 in 331 human astrocytomas . ^^^ The focal adhesion kinase ( FAK ) and the proline rich tyrosine kinase ( Pyk 2 ) show a high expression in glioma cell lines and have an influence on increased cell proliferation and migration of glioma cells in vitro and in vivo . ^^^ The aim of this study was to correlate the coexpression of FAK and Pyk 2 to the WHO grade of malignancy in human astrocytomas . ^^^ Immunohistochemical staining scores of FAK and Pyk 2 were analyzed in 331 astrocytomas and correlated to each other and to the WHO grade . ^^^ Significant coexpression of FAK and Pyk 2 in astrocytomas was demonstrated . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In addition to interactions with multiple signaling adaptors Grb 2 , SHC , SCK , and NSP 2 , EGF receptors in HN 5 cells were shown to form direct or indirect physical interactions with additional kinases including ACK 1 , focal adhesion kinase ( FAK ) , Pyk 2 , Yes , EphA 2 , and EphB 4 . ^^^ Focal adhesion proteins , FAK , Pyk 2 , paxillin , ARF / GIT1 , and plakophillin were down regulated by transient EGF stimulation suggesting a complex balance between growth factor induced kinase and phosphatase activities in the control of cell adhesion complexes . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Transient forebrain ischemia effects interaction of Src , FAK , and PYK 2 with the NR2B subunit of N methyl D aspartate receptor in gerbil hippocampus . ^^^ Two different models of brain ischemia were used to examine the evoked changes in the tyrosine phosphorylation of NMDA receptor subunits 2A and 2B ( NR2A and NR2B ) , as well as their interactions with non receptor tyrosine kinases ( NRTKs : FAK , PYK 2 Src ) , and PSD 95 protein . ^^^ Concomitantly , an increased association of NR2B with FAK , PYK 2 , Src and PSD 95 has been observed . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| It involves translocation ( i . e . activation ) of PKCalpha from the cytosol to the membrane and / or the Triton 10 100 insoluble subcellular fractions , with recruitment into a complex with alphaVbeta 3 integrin , growth factor receptor bound protein ( Grb 2 ) , focal adhesion kinase ( FAK ) in CHO cells and proline rich tyrosine kinase ( PYK 2 ) in osteoclasts . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Ang 2 induced AT1R activation via Gq / 11 stimulates phospholipases A 2 , C , and D , and activates inositol trisphosphate / Ca2+ signaling , protein kinase C isoforms , and MAPKs , as well as several tyrosine kinases ( Pyk 2 , Src , Tyk 2 , FAK ) , scaffold proteins ( G protein coupled receptor kinase interacting protein 1 , p130Cas , paxillin , vinculin ) , receptor tyrosine kinases , and the nuclear factor kappaB pathway . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Under conditions of low concentrations of ECM , invasin was found to be the dominant adhesin , promoting high levels of phagocytosis coincident with robust and sustained activation of the protein tyrosine kinases Fak and Pyk 2 , phosphorylation of the adaptor molecule Cas and activation of the small GTPase Rac 1 . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Herein , we show that FAK expression is essential for alpha5beta1 stimulated cell motility and that exogenous expression of human alpha 4 in FAK null fibroblasts forms a functional alpha4beta1 receptor that promotes robust cell motility equal to the alpha5beta1 stimulation of wild type and FAK reconstituted fibroblasts . alpha4beta1 stimulated FAK null cell spreading and motility were dependent on the integrity of the alpha 4 cytoplasmic domain , independent of direct paxillin binding to alpha 4 , and were not affected by PRNK expression , a dominant negative inhibitor of Pyk 2 . alpha 4 cytoplasmic domain initiated signaling led to a approximately 4 fold activation of c Src which did not require paxillin binding to alpha 4 . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Infection of Du 3 cells induced the phosphorylation of the FAK related proline rich tyrosine kinase ( Pyk 2 ) molecule , which has been shown to complement some of the functions of FAK . ^^^ Expression of an autophosphorylation site mutant of Pyk 2 in which Y 402 is mutated to F ( F 402 Pyk2 ) reduced viral entry in Du 3 cells , suggesting that Pyk 2 facilitates viral entry moderately in the absence of FAK . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In vascular smooth muscle cells ( VSMCs ) , through its G protein coupled AngII Type 1 receptor ( AT ( 1 ) ) , AngII activates various intracellular protein kinases , such as receptor or non receptor tyrosine kinases , which includes epidermal growth factor receptor ( EGFR ) , platelet derived growth factor receptor ( PDGFR ) , c Src , PYK 2 , FAK , JAK 2 . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We showed that cyclic strain ( CS ) of osteoblastic cells induced tyrosine phosphorylation of two homologous tyrosine kinases FAK and PYK 2 , and of two homologous adaptor proteins paxillin and Hic 5 , with similar kinetics . ^^^ While FAK and paxillin remained at the focal contact , Hic 5 and PYK 2 translocated outside ventral focal contacts as early as 30 min after CS and were sequestered by the cytoskeleton . ^^^ Altogether these results suggested that CS regulates focal contact activity in osteoblasts by modulating PYK 2 containing complexes in particular by shuttling out of the focal contact the adaptor Hic 5 and favoring the anchorage of FAK within contacts . . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| CCK stimulated an association of Lyn with PKC delta , Shc , p 125 ( FAK ) and PYK 2 as well as with their autophosphorylated forms , but not with Cbl , p 85 , p 130 ( CAS ) or ERK 1 / 2 . ^^^ CCK ' s activation of Lyn is likely an important mediator of its ability to cause tyrosine phosphorylation of numerous important cellular mediators such as p 125 ( FAK ) , PYK 2 , PKC delta and Shc , which play central roles in CCK ' s effects on acinar cell function . . ^^^ |
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| Interacting proteins: Q14289 and Q05397 |
Pubmed |
SVM Score :0.0 |
| RESULTS : A single orthologue of FAK and the related PYK 2 was found in non vertebrate species . ^^^ The amino acid sequence of FAK and PYK 2 is conserved in their functional domains but not in their linker regions , with the absence of autophosphorylation site in C . elegans . ^^^ |
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