Redox regulation of protein-tyro sine phosphatases

被引：124

作者：

den Hertog, J ^{[1
]}

Groen, A ^{[1
]}

van der Wijk, T ^{[1
]}

机构：

[1] Netherlands Inst Dev Biol, Hubrecht Lab, NL-3584 CT Utrecht, Netherlands

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2005年 / 434卷 / 01期

关键词：

protein-tyrosine phosphatase; regulation; oxidation; redox; conformational change; dimerization;

D O I：

10.1016/j.abb.2004.05.024

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 protein-tyrosine phosphatases (PTPs) form a large family of signaling proteins with essential functions in embryonic development and adult physiology. The PTPs are characterized by an absolutely conserved catalytic site cysteine with a low pK(a) due to its microenvironment, making it vulnerable to oxidation. PTPs are differentially oxidized and inactivated in vitro and in living cells. Many cellular stimuli induce a shift in the cellular redox state towards oxidation and evidence is accumulating that at least part of the cellular responses to these stimuli are due to specific, transient inactivation of PTPs, indicating that PTPs are important sensors of the cellular redox state. (C) 2004 Elsevier Inc. All rights reserved.

引用

页码：11 / 15

页数：5

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