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Sci. Signal., 31 August 2010
Vol. 3, Issue 137, p. pl2
[DOI: 10.1126/scisignal.3137pl2]


Targeting the Reversibly Oxidized Protein Tyrosine Phosphatase Superfamily

Benoit Boivin1, Ming Yang1,2, and Nicholas K. Tonks1*

1 Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
2 Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794–5215, USA.

Abstract: Controlled production of reactive oxygen species leads to reversible oxidation of protein tyrosine phosphatases (PTPs) and has emerged as an important tier of regulation over phosphorylation-dependent signal transduction. We present a modified cysteinyl-labeling assay that detects reversible oxidation of members of each of the different PTP subclasses. Here, we describe the methods for enriching reversibly oxidized PTPs from complex protein extracts, illustrating the procedure in IMR90 fibroblasts.

* Corresponding author. Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724–2202, USA. E-mail, tonks{at}

Citation: B. Boivin, M. Yang, N. K. Tonks, Targeting the Reversibly Oxidized Protein Tyrosine Phosphatase Superfamily. Sci. Signal. 3, pl2 (2010).

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