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含 SH2 和 PTB 结构域的蛋白质在受体酪氨酸激酶信号转导中的分子机制。

Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.

机构信息

Lunenfeld Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, Ontario M5G 1X5, Canada.

出版信息

Cold Spring Harb Perspect Biol. 2013 Dec 1;5(12):a008987. doi: 10.1101/cshperspect.a008987.

Abstract

Intracellular signaling is mediated by reversible posttranslational modifications (PTMs) that include phosphorylation, ubiquitination, and acetylation, among others. In response to extracellular stimuli such as growth factors, receptor tyrosine kinases (RTKs) typically dimerize and initiate signaling through phosphorylation of their cytoplasmic tails and downstream scaffolds. Signaling effectors are recruited to these phosphotyrosine (pTyr) sites primarily through Src homology 2 (SH2) domains and pTyr-binding (PTB) domains. This review describes how these conserved domains specifically recognize pTyr residues and play a major role in mediating precise downstream signaling events.

摘要

细胞内信号转导是由可逆的翻译后修饰(PTMs)介导的,包括磷酸化、泛素化和乙酰化等。在生长因子等细胞外刺激的作用下,受体酪氨酸激酶(RTKs)通常通过其细胞质尾部和下游支架的磷酸化二聚化并启动信号转导。信号效应物主要通过Src 同源 2(SH2)结构域和磷酸酪氨酸结合(PTB)结构域募集到这些磷酸酪氨酸(pTyr)位点。本文综述了这些保守结构域如何特异性识别 pTyr 残基,并在介导精确的下游信号事件中发挥主要作用。

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