Gathering STYX: phosphatase like form predicts functions for unique protein-interaction domains

被引：111

作者：

Wishart, MJ ^{[1
]}

Dixon, JE

机构：

[1] Univ Michigan, Dept Physiol, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Dept Biol Chem, Ann Arbor, MI 48109 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1998年 / 23卷 / 08期

关键词：

D O I：

10.1016/S0968-0004(98)01241-9

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：

The effects of tyrosine phosphorylation are manifested and regulated through protein domains that bind to specific phosphotyrosine motifs. STYX is a unique modular domain found within proteins implicated in mediating the effects of tyrosine phosphorylation in vivo. Individual STYX domains are not catalytically active; however, they resemble protein tyrosine phosphatase (PTP) domains and, like PTPs, contain core sequences that recognize phosphorylated substrates. Thus, the STYX domain adds to the repertoire of modular domains that can mediate intracellular signaling in response to protein phosphorylation.

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收藏

页码：301 / 306

页数：6

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