Redox regulation of PTEN and protein tyrosine phosphatases in H2O2‐mediated cell signaling

FEBS Letters

Cho, Seung-Hyun²  Ahn, Chi-Young¹  Kim, Hoeon¹  Ahn, Younghee²  Lee, Seung-Rock²  Kim, Hyunjung²  Lee, Chang-Hun²  Yang, Kap-Seok² 

[1] Research Institute of Biotechnology, Histochem, Inc., 518-45, Doonchun-dong, Kangdong-gu, Seoul 134-060, South Korea;Center for Cell Signaling Research, Division of Molecular Life Sciences, Department of Biological Sciences, Ewha Women's University, Seoul 120-750, South Korea

关键词: Protein tyrosine phosphatase;    PTEN;    Cdc25;    Low molecular weight protein tyrosine phosphatase;    Disulfide bond;    Redox regulation;    Hydrogen peroxide;    PTP;    protein tyrosine phosphatase;    PDGF;    platelet-derived growth factor;    EGF;    epidermal growth factor;    PIP3;    phosphatidylinositol 3;    4;    5-trisphosphate;   

DOI  :  10.1016/S0014-5793(04)00112-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 H₂O₂ 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 H₂O₂. 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.

【 授权许可】

Unknown