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Negative regulation of cytoplasmic protein tyrosinekinase activity by adaptor proteins

机译:衔接蛋白对细胞质蛋白酪氨酸激酶活性的负调控

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Adaptor proteins are cytoplasmic signaling molecules that lack intrinsic catalytic activity but they are nevertheless crucial for signal transduction. They bear homology domains (SH2, SH3, PH, PTB, ...) important for protein- protein interactions and for function. The first adaptors identified were positive regulators of cell responses, with some even having oncogenic activities. More recently, a new subfamily has emerged that negatively regulates signaling responses. This review will focus on adaptors of this genre and specifically, those that inhibit cytoplasmic tyrosine kinase function and which define a new mechanism for in vivo kinase regulation. They include the inhibitors of the Jak, Syk, Fak and Src kinase family and their mechanism for inhibition as well as their possible function in cellular regulation will be discussed.
机译:衔接子蛋白是缺乏内在催化活性的细胞质信号分子,但是它们对于信号转导仍然至关重要。它们具有同源结构域(SH2,SH3,PH,PTB等),对蛋白质-蛋白质相互作用和功能至关重要。鉴定出的第一个衔接子是细胞反应的正调节剂,其中一些甚至具有致癌活性。最近,出现了一个新的亚家族,它负面调节信号传导反应。这篇综述将集中在这种类型的衔接子上,尤其是那些抑制细胞质酪氨酸激酶功能并为体内激酶调节定义新机制的衔接子。它们包括Jak,Syk,Fak和Src激酶家族的抑制剂,并将讨论其抑制机理以及它们在细胞调节中的可能功能。

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