Focal adhesion kinase signal transduction and crosstalk Research.docVIP

 PAGE \* MERGEFORMAT 10 Focal adhesion kinase signal transduction and crosstalk Research [Keywords:] focal adhesion kinase [Keywords:] focal adhesion kinase; signal transduction; cross-talk Progress in research on focal adhesion kinase signal transduction and crosstalk Focal adhesion kinase (focal adhesion kinase, FAK) is a cytoplasmic non-receptor tyrosine kinase, molecular weight 125 kD, the lack of transmembrane domain [1], but contains the SH2 and SH3 binding sequence. It contains six tyrosine can be phosphorylated, namely, Tyr397, Tyr407, Tyr576, Tyr577, Tyr861, Tyr925. N-terminal Tyr397 is a major self-phosphorylation sites may be Src family (Src, Yes, Fyn, etc.) of the SH2 domain binding; in the kinase domain activation loop Tyr576 and Tyr577 within the Src family kinase phosphorylation is the main part of [2 ], followed by the carboxy-terminal Tyr861 and Tyr925, Tyr861 phosphorylation may be involved in fibroblast cells, Ras signaling pathway [3], Tyr925 phosphorylation may participate in PDE alpha / ATX regulation of myelin-forming process [4]. Integrins, growth factors, mechanical stimuli (stretch), hypertonic pressure and other factors can activate FAK [5,6], induced rapid phosphorylation of Tyr397 and Tyr577. When the integrin-binding extracellular matrix components, its β subunit intracellular domain and the FAK amino-terminal binding, carboxy-terminal FAK and focal adhesion convergence, kinase domain is activated state, the temporary role of FAK molecules leading to dimerization Tyr397 phosphorylation between molecules [7], and, Tyr861 high degree of phosphorylation, may contribute to Tyr397 phosphorylation [8], Tyr397 phosphorylation resulting from self-Src family kinases with high affinity sites, forming FAKSrc signal transduction complex. The regulation of Src C-terminal of Tyr397 of FAK tyrosine has been replaced has been activated; activated Src catalytic FAK others, especially Tyr576, and Tyr577 tyrosine phosphorylation sites, so that