C-terminal binding: An expanded repertoire and function of 14-3-3 proteins

被引：136

作者：

Coblitz, B ^{[1
]}

Wu, M ^{[1
]}

Shikano, S ^{[1
]}

Li, M ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Neurosci & High Throughput Biol Ctr, Baltimore, MD 21205 USA

来源：

FEBS LETTERS | 2006年 / 580卷 / 06期

关键词：

14-3-3; binding motif; mode III; cancer signaling; C-terminal; SWTY; phosphorylation; binding assay; fluorescence anisotropy;

D O I：

10.1016/j.febslet.2006.02.014

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：

Amino and carboxyl termini are unique positions in a polypeptide. They tend to be exposed in folded three dimensional structures. Diversity and functional significance of C-terminal sequences have been appreciated from studies of PDZ and PEX domains. Signaling 14-3-3 protein signaling by recognizing phosphorylated peptides plays a critical role in a variety of biological processes, including oncogenesis. The preferential binding of 14-3-3 to phosphorylated C-terminal sequences, mode III, provides a means of regulated binding and considerably expands the substrate repertoire of 14-3-3 interaction partners. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：1531 / 1535

页数：5

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