B cell antigen receptor stimulation induces formation of a Shc-Grb2 complex containing multiple tyrosine-phosphorylated proteins.

作者: J. Borst , L. Smit , A. M. M. De Vries-Smits , J. L. Bos

DOI: 10.1016/S0021-9258(17)31975-0

关键词: SH2 domainReceptor tyrosine kinaseTyrosine phosphorylationCell surface receptorMolecular biologyROR1Platelet-derived growth factor receptorProtein tyrosine phosphataseBiologyTyrosine kinase

摘要: Activation of growth factor receptor tyrosine kinases, such as the epidermal and insulin receptors, induces phosphorylation Shc proteins their association with SH2 domain-containing adaptor protein Grb2. The Shc-Grb2 complex has been implicated in coupling these receptors to p21ras. B cell antigen plays a key role directing proliferation differentiation. Although lacks intrinsic kinase activity, its mode action parallels that kinases many aspects. stimulation activates src-related syk, which leads various cytoplasmic initiates multiple signaling events, including p21ras activation. Therefore, we have investigated whether are targets for activated receptor. It was found 52- 46-kDa forms expressed mature human cells become rapidly phosphorylated on upon stimulation. Also, is induced associate Grb2 molecule an undefined 130-kDa protein. In specific response activation, associates several tyrosine-phosphorylated proteins, two prominent phosphoproteins molecular masses 130 110 kDa. These observations strongly suggest involved one or signal transduction pathways.

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