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
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: | https://repository.cshl.edu/id/eprint/28746 |
Actions (login required)
 |
Administrator's edit/view item |
