Autoinhibition of Sos by intramolecular interactions

被引：11

作者：

Hall, BE

Yang, SS

Sagi, DB

机构：

[1] SUNY Stony Brook, Dept Mol Genet & Microbiol, Stony Brook, NY 11794 USA

[2] SUNY Stony Brook, Grad Programs Mol Pharmacol, Stony Brook, NY 11794 USA

[3] SUNY Stony Brook, Grad Programs Mol & Cellular Biol, Stony Brook, NY 11794 USA

来源：

FRONTIERS IN BIOSCIENCE | 2002年 / 7卷

关键词：

Ras; Sos; autoinhibition; receptor tyrosine kinase; guanine nucleotide exchange; intramolecular interaction; review;

D O I：

10.2741/hall

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Sos proteins function as activators of Ras signaling by catalyzing guanine nucleotide exchange on Ras. Sos regulation was initially thought to be accomplished primarily through its growth factor-dependent recruitment to the plasma membrane. More recent data has indicated that while membrane association is an indispensable means of Sos regulation, additional mechanisms involving intramolecular interactions function to control Sos activity towards Ras. This review will examine the experimental evidence for Sos intramolecular interactions and their contribution to Sos regulation.

引用

页码：D288 / D294

页数：7

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[1] Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities [J].