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受体酪氨酸激酶介导的信号复合物组装

The assembly of signalling complexes by receptor tyrosine kinases.

作者信息

Panayotou G, Waterfield M D

机构信息

Ludwig Institute for Cancer Research, University College, Middlesex Hospital Branch, London, U.K.

出版信息

Bioessays. 1993 Mar;15(3):171-7. doi: 10.1002/bies.950150305.

Abstract

Cell proliferation in response to growth factors is mediated by specific high affinity receptors. Ligand-binding by receptors of the protein tyrosine kinase family results in the stimulation of several intracellular signal transduction pathways. Key signalling enzymes are recruited to the plasma membrane through the formation of stable complexes with activated receptors. These interactions are mediated by the conserved, non-catalytic SH2 domains present in the signalling molecules, which bind with high affinity and specificity to tyrosine-phosphorylated sequences on the receptors. The assembly of enzyme complexes is emerging as a major mechanism of signal transduction and may regulate the pleiotropic effects of growth factors.

摘要

细胞对生长因子的增殖反应由特定的高亲和力受体介导。蛋白质酪氨酸激酶家族受体与配体结合会刺激多种细胞内信号转导途径。关键信号酶通过与活化受体形成稳定复合物而被招募到质膜。这些相互作用由信号分子中保守的非催化性SH2结构域介导,该结构域以高亲和力和特异性与受体上的酪氨酸磷酸化序列结合。酶复合物的组装正成为信号转导的主要机制,并可能调节生长因子的多效性作用。

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