| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| LAD PMNs did not adhere to LN , and consequently , there was no tyrosine phosphorylation of FAK or paxillin . ^^^ In contrast , paxillin , but not FAK , was phosphorylated in LAD PMNs adherent and spread on TSP . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| In contrast , in thymocytes stimulation of VLA 4 ( alpha 4 beta 1 ) and LFA 1 ( alpha L beta 2 ) resulted in a marked decrease in tyrosine phosphorylation and activity of FAK . . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| These data indicate that the beta 2 integrin LFA 1 expressed on T lymphocytes stimulates a novel , FAK related molecule that may function in the interplay between adhesion receptors and intracellular signaling enzymes responsible for downstream second messenger generation . . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Beta 2 integrin , LFA 1 , and TCR / CD3 synergistically induce tyrosine phosphorylation of focal adhesion kinase ( pp 125 ( FAK ) ) in PHA activated T cells . ^^^ Although signaling through beta 1 or beta 3 integrins induces tyrosine phosphorylation of FAK , there has been no evidence that activation of T cells through the beta 2 integrin , LFA 1 , involves FAK . ^^^ We report here that crosslinking of LFA 1 induces tyrosine phosphorylation of FAK in PHA activated T cells . ^^^ Moreover , cocrosslinking with anti LFA 1 mAb and suboptimal concentration of anti CD 3 mAb markedly increases tyrosine phosphorylation of FAK in an antibody concentration dependent and time kinetics dependent manner compared with stimulation through CD 3 alone , which correlates well with enhanced proliferation of PHA activated T cells . ^^^ These results indicate , for the first time , that signals mediated by LFA 1 can regulate FAK , suggesting that LFA 1 mediated T cell costimulation may be involved in T cell activation at least partially through FAK . . ^^^ |
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| Interacting proteins: P05107 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 ) . ^^^ Our results demonstrate that interaction of the beta 2 integrin LFA 1 with its ligand intercellular adhesion molecule 1 induces remodeling of T lymphocyte morphology and activation and redistribution of the cytoplasmic tyrosine kinases FAK and PYK 2 . . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| We report here that crosslinking of LFA 1 induces tyrosine phosphorylation of FAK in PHA activated T cells . ^^^ Moreover , co crosslinking with anti LFA 1 monoclonal antibody ( mAb ) and suboptimal concentration of anti CD 3 mAb markedly increases tyrosine phosphorylation of FAK in an antibody concentration and time dependent manner compared with stimulation through CD 3 alone . ^^^ Results indicate that signals mediated by LFA 1 can regulate FAK , suggesting that LFA 1 mediated T cell costimulation may be involved in T cell activation at least partially through FAK . . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Herein , we investigate the role of a FAK tyrosine phosphatase , namely low molecular weight phosphotyrosine phosphatase ( LMW PTP ) , in the modulation of LFA 1 mediated T cell adhesion . ^^^ Our results also demonstrated that , upon antigen stimulation , LMW PTP dependent FAK inhibition is associated to a strong reduction of LFA 1 and TCR co clustering toward a single region of T cell surface , thus causing an impairment of receptor activity by preventing changes in their avidity state . ^^^ Because co localization of both LFA 1 and TCR is an essential event during encounters of T cells with antigen presenting cells and immunological synapse ( IS ) formation , we suggest an intriguing role of LMW PTP in IS establishment and stabilization through the negative control of FAK activity and , in turn , of cell surface receptor redistribution . . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| This process involved their interaction with LFA 1 integrin , but no subsequent p ( 125 ) FAK phosphorylation . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| Phosphorylation of focal adhesion kinase ( FAK ) and mitogen activated protein kinase ( MAPK ) was increased in Mac 1 uPAR co transfected cells but not in Mac 1 transfected cells . ^^^ CONCLUSIONS : uPAR up regulated the Mac 1 adhesion to fibrinogen and FAK and MAPK were involved in this regulation . . ^^^ |
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| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P05107 and Q05397 |
Pubmed |
SVM Score :0.0 |
| NA |
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