p56lck CONTROLS PHOSPHORYLATION OF FILAMIN (ABP-280) AND REGULATES FOCAL ADHESION KINASE (pp125FAK)
作者： W Goldmann
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摘要: Transformation of cells by src -like kinases leads to altered cell morphology associated with the disassembly focal contacts and concomitant increase in tyrosine phosphorylation pp125FAK. p56lck is a lymphocyte-specific member family protein that associates surface glycoproteins such as CD4 CD8. It phosphorylates activates pp125FAK increases its autokinase activity, thus pretreatment kinase C (PKC) markedly attenuates activation, suggesting potential regulatory pathway activation contacts. further actin binding (ABP-280; filamin) controls association receptors β-2 integrins, filament cross-linking, possibly lipid membrane insertion.
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