Modulation of tyrosine phosphorylation of p36 and other substrates by the S-100 protein.
作者： M Hagiwara , M Ochiai , K Owada , T Tanaka , H Hidaka
DOI: 10.1016/S0021-9258(18)68805-2
关键词:
摘要: The inhibitory effects of Ca2+-binding proteins on tyrosine phosphorylation p36 protein isolated from bovine intestinal epithelium by immunoprecipitated p130fps were investigated. S-100 dose dependently inhibited the phosphorylation, and calmodulin weakly depressed whereas parvalbumin troponin C had no significant effects. preparation purified brain did not contain phosphatase activity or ATPase activity. concentration ATP affect S-100-mediated inhibition but substrate protein, p36, reversed inhibition. similarly p60src kinase C. using other substrates tested as well. These results suggest that interacts with binding site retroviral tyrosine-specific kinases may play a regulatory role in phosphorylation.
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