Redox regulation of PTEN and protein tyrosine phosphatases in H(2)O(2) mediated cell signaling.

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作者：

SH Cho，CH Lee，Y Ahn，H Kim，H Kim，CY Ahn，KS Yang，SR Lee

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摘要：

Protein tyrosine phosphatase (PTP) is a family of enzymes important for regulating cellular phosphorylation state. The oxidation and consequent inactivation of several PTPs by H 2O 2 are well demonstrated. It is also shown that recovery of enzymatic activity depends on the availability of cellular reductants. Among these redox-regulated PTPs, PTEN, Cdc25 and low molecular weight PTP are known to form a disulfide bond between two cysteines, one in the active site and the other nearby, during oxidation by H 2O 2. The disulfide bond likely confers efficiency in the redox regulation of the PTPs and protects cysteine-sulfenic acid of PTPs from further oxidation. In this review, through a comparative analysis of the oxidation process of Yap1 and PTPs, we propose the mechanism of disulfide bond formation in the PTPs.

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关键词：

PTP, protein tyrosine phosphatase PDGF, platelet-derived growth factor EGF, epidermal growth factor PIP 3, phosphatidylinositol 3,4,5-trisphosphate

DOI：

10.1016/S0014-5793(04)00112-7

被引量：

494

年份：

2004