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在成纤维细胞生长因子(FGF)刺激的细胞中,SHP2直接与酪氨酸磷酸化的p90(SNT)蛋白结合。

SHP2 associates directly with tyrosine phosphorylated p90 (SNT) protein in FGF-stimulated cells.

作者信息

Ong S H, Lim Y P, Low B C, Guy G R

机构信息

Signal Transduction Laboratory, Institute of Molecular and Cell Biology, Singapore.

出版信息

Biochem Biophys Res Commun. 1997 Sep 8;238(1):261-6. doi: 10.1006/bbrc.1997.7272.

Abstract

In a number of cell lines responsive to basic fibroblast growth factor (bFGF), two major tyrosine phosphorylated proteins, of molecular weights around 120kDa and 90kDa, are precipitated along with the tyrosine phosphatase SHP2 from the lysates of stimulated cells. The docker protein Gab-1 represents at least part of the 120kDa protein(s). The p90 protein was identified as the SNT protein. The two SH2 domains of SHP2 bind directly and synergistically to tyrosine phosphorylated SNT. Tyrosine phosphorylated SNT does not bind SHP1 and does not appear to be an in vivo substrate of SHP2 but is likely to function as an adapter protein in FGF-signalling.

摘要

在一些对碱性成纤维细胞生长因子(bFGF)有反应的细胞系中,从受刺激细胞的裂解物中沉淀出两种主要的酪氨酸磷酸化蛋白,分子量分别约为120kDa和90kDa,同时还有酪氨酸磷酸酶SHP2。停泊蛋白Gab-1至少代表了120kDa蛋白的一部分。p90蛋白被鉴定为SNT蛋白。SHP2的两个SH2结构域直接且协同地与酪氨酸磷酸化的SNT结合。酪氨酸磷酸化的SNT不与SHP1结合,似乎也不是SHP2在体内的底物,但可能在FGF信号传导中作为衔接蛋白发挥作用。

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