GATHERING STYX - PHOSPHATASE LIKE FORM PREDICTS FUNCTIONS FOR UNIQUE PROTEIN-INTERACTION DOMAINS

Citation
Mj. Wishart et Je. Dixon, GATHERING STYX - PHOSPHATASE LIKE FORM PREDICTS FUNCTIONS FOR UNIQUE PROTEIN-INTERACTION DOMAINS, Trends in biochemical sciences, 23(8), 1998, pp. 301-306
Citations number
47
Categorie Soggetti
Biology
ISSN journal
09680004
Volume
23
Issue
8
Year of publication
1998
Pages
301 - 306
Database
ISI
SICI code
0968-0004(1998)23:8<301:GS-PLF>2.0.ZU;2-F
Abstract
The effects of tyrosine phosphorylation are manifested and regulated t hrough protein domains that bind to specific phosphotyrosine motifs. S TYX is a unique modular domain found within proteins implicated in med iating the effects of tyrosine phosphorylation in vivo. Individual STY X domains are not catalytically active; however, they resemble protein tyrosine phosphatase (PTP) domains and, like PTPs, contain core seque nces that recognize phosphorylated substrates. Thus, the STYX domain a dds to the repertoire of modular domains that can mediate intracellula r signaling in response to protein phosphorylation.