Buday L
Department of Medical Chemistry, Semmelweis University Medical School, 9 Puskin Street, 1088, Budapest, Hungary.
Biochim Biophys Acta. 1999 Jul 6;1422(2):187-204. doi: 10.1016/s0304-4157(99)00005-2.
SH2/SH3 domain-containing adaptor proteins play a critical role in regulating tyrosine kinase signalling pathways. The major function of these adaptors, such as Grb2, Nck, and Crk, is to recruit proline-rich effector molecules to tyrosine-phosphorylated kinases or their substrates. In recent years dozens of novel proteins have emerged that are capable of associating with the SH2 and the SH3 domains of adaptors. In this review, the author attempts to summarise these novel binding partners of Grb2, Nck, and Crk, and to discuss current controversies regarding function and regulation of protein multicomplexes held together by SH2/SH3 adaptor molecules at the plasma membrane.
含SH2/SH3结构域的衔接蛋白在调节酪氨酸激酶信号通路中起关键作用。这些衔接蛋白,如Grb2、Nck和Crk的主要功能是将富含脯氨酸的效应分子招募到酪氨酸磷酸化的激酶或其底物上。近年来,出现了数十种能够与衔接蛋白的SH2和SH3结构域结合的新型蛋白质。在这篇综述中,作者试图总结Grb2、Nck和Crk的这些新型结合伴侣,并讨论目前关于质膜上由SH2/SH3衔接分子维系的蛋白质多聚复合体的功能和调控的争议。