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. 2002 Feb;9(2):387-99.
doi: 10.1016/s1097-2765(02)00445-8.

Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo

Tzu-Ching Meng  1 , Toshiyuki Fukada, Nicholas K Tonks
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Free article

Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo

Tzu-Ching Meng et al. Mol Cell. 2002 Feb.
Free article

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 H(2)O(2) 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.

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