Inhibition of c-Abl tyrosine kinase activity by filamentous actin.
作者： Pamela J. Woodring , Tony Hunter , Jean Y. J. Wang
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摘要: The catalytic activity of c-Abl tyrosine kinase is reduced in fibroblasts that are detached from the extracellular matrix. We report here a deletion extreme C terminus (DeltaF-actin c-Abl) can partially restore to cells. Because contains consensus F-actin binding motif, we investigated effect on activity. found inhibit purified protein. Mutations C-terminal region disrupted both and inhibition by F-actin. SH3, SH2, DNA domains did not abolish Catalytic domain substitutions affect regulation retinoblastoma protein or ataxia telangiectasia-mutated also Interestingly, among these mutants, only DeltaF-actin retained Taken together, data suggest an inhibitor this contributes part Abl
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