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p56 lck CONTROLS PHOSPHORYLATION OF FILAMIN (ABP‐280) AND REGULATES FOCAL ADHESION KINASE (pp125 FAK )
Author(s) -
Goldmann Wolfgang H.
Publication year - 2002
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.2002.0900
Subject(s) - focal adhesion , filamin , tyrosine phosphorylation , phosphorylation , microbiology and biotechnology , proto oncogene tyrosine protein kinase src , tyrosine kinase , chemistry , integrin , kinase , signal transduction , biology , cell , cytoskeleton , biochemistry
Transformation of cells by src ‐like kinases leads to altered cell morphology associated with the disassembly of focal contacts and concomitant increase in tyrosine phosphorylation of pp125 FAK . p56 lck is a lymphocyte‐specific member of the src family of protein tyrosine kinases that associates with cell surface glycoproteins such as CD4 and CD8. It phosphorylates and activates pp125 FAK and increases its autokinase activity, thus pretreatment of pp125 FAK with protein kinase C (PKC) markedly attenuates its phosphorylation and activation, suggesting a potential regulatory pathway of pp125 FAK activation in focal contacts. p56 lck further phosphorylates and activates actin binding protein (ABP‐280; filamin) and controls its association with cell surface receptors such as β‐2 integrins, actin filament cross‐linking, and possibly lipid membrane insertion.