Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo

Meng, T. C., Fukada, T., Tonks, N. K. (February 2002) Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Molecular Cell, 9 (2). pp. 387-399. ISSN 1097-2765

URL: http://www.ncbi.nlm.nih.gov/pubmed/11864611
DOI: 10.1016/S1097-2765(02)00445-8

Abstract

We have investigated the regulation of protein tyrosine phosphatases (PTPs) by reactive oxygen species (ROS) in a cellular environment. We demonstrate that multiple PTPs were reversibly oxidized and inactivated following treatment of Rat-1 cells with H2O2 and that inhibition of PTP function was important for ROS-induced mitogenesis. Furthermore, we show transient oxidation of the SH2 domain containing PTP, SHP-2, in response to PDGF that requires association with the PDGFR. Our results indicate that SHP-2 inhibits PDGFR signaling and suggest a mechanism by which autophosphorylation of the PDGFR occurs despite its association with SHP-2. The data suggest that several PTPs may be regulated by oxidation and that characterization of this process may define novel links between specific PTPs and particular signaling pathways in vivo.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
diseases & disorders > pulmonary disease > oxidative stress
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: February 2002
Date Deposited: 16 Dec 2013 17:43
Last Modified: 16 Dec 2013 17:43
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28746

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