Work

Targeting the Reversibly Oxidized Protein Tyrosine Phosphatase Superfamily

Year: 2010

Type: article

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.

Source: Science Signaling

DOI: 10.1126/scisignal.3137pl2

Authors: Benoit Boivin, Ming Yang, Nicholas K. Tonks

Institutions: Cold Spring Harbor Laboratory, Stony Brook University

Language: English

Topic: Protein Tyrosine Phosphatases

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Award: Receptor PTPs, Cell Contact and Signal Transduction