Ras recruits Raf‐1 to the plasma membrane for activation by tyrosine phosphorylation.

作者: R. Marais , Y. Light , H.F. Paterson , C.J. Marshall

DOI: 10.1002/J.1460-2075.1995.TB07316.X

关键词: SH2 domainProto-oncogene tyrosine-protein kinase SrcTyrosine kinaseTyrosine phosphorylationReceptor tyrosine kinaseTyrosine-protein kinase CSKBiochemistrySH3 domainProtein tyrosine phosphataseCell biologyBiology

摘要: A central feature of signal transduction downstream both receptor and oncogenic tyrosine kinases is the Ras-dependent activation a protein kinase cascade consisting Raf-1, Mek (MAP kinase) ERKs kinases). To study role activity in we have examined properties p74Raf-1 Src that are necessary for p74Raf-1. We show mammalian cells by requires pp60Src to be myristoylated ability interact with p21Ras-GTP. The Ras/Raf interaction required p21Ras-GTP bring plasma membrane phosphorylation at 340 or 341, probably membrane-bound pp60Src. When expressed activated 5-fold; however, when co-expressed Ras Src, Raf-1 25-fold this associated further 3-fold increase phosphorylation. Thus, limiting component bringing Using mutants Tyr340/341, addition these sites, there an additional step resulting from recruiting membrane. least two different steps.

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