PMID: 7525585Nov 25, 1994Paper

Evidence for two distinct 60-kilodalton substrates of the SRC tyrosine kinase

The Journal of Biological Chemistry
W OgawaR A Roth

Abstract

A monoclonal antibody to a 60-kDa substrate of the insulin receptor tyrosine kinase is utilized in the present studies to examine this molecule in 3T3 cells expressing either the transforming chicken c-Src (mutant Phe-527), the wild type molecule, or the parental cells. The tyrosine phosphorylation of this 60-kDa protein was greatly increased in cells expressing transforming Src and partially increased in cells expressing wild type enzyme. This tyrosine phosphorylation correlated with an increased association with the GTPase-activating protein of p21ras (GAP). However, this 60-kDa protein did not react with antibodies to another 62-kDa tyrosine-phosphorylated protein previously isolated from Src-transformed cells (Wong, G., Muller, O., Clark, R., Conroy, L., Moran, M. F., Polakis, P., and McCormick, F. (1992) Cell 69, 551-558), although this latter antibody did react with a 62-kDa protein in anti-phosphotyrosine precipitates from cells expressing transforming c-Src but not the parental cells. These two proteins could also be distinguished by their subcellular location, the ability of the latter but not the former protein to bind RNA, and their migration in SDS gels. Moreover, the 62-kDa RNA-binding phosphoprotein could be almos...Continue Reading

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