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Cell. 2011 Sep 2;146(5):826-40. doi: 10.1016/j.cell.2011.07.020.

Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome".

Author information

1
Department of Medical Biophysics, University of Toronto, Toronto M5G 2M9, ON, Canada. rkarisch@uhnresearch.ca

Abstract

Protein-tyrosine phosphatases (PTPs), along with protein-tyrosine kinases, play key roles in cellular signaling. All Class I PTPs contain an essential active site cysteinyl residue, which executes a nucleophilic attack on substrate phosphotyrosyl residues. The high reactivity of the catalytic cysteine also predisposes PTPs to oxidation by reactive oxygen species, such as H(2)O(2). Reversible PTP oxidation is emerging as an important cellular regulatory mechanism and might contribute to diseases such as cancer. We exploited these unique features of PTP enzymology to develop proteomic methods, broadly applicable to cell and tissue samples, that enable the comprehensive identification and quantification of expressed classical PTPs (PTPome) and the oxidized subset of the PTPome (oxPTPome). We find that mouse and human cells and tissues, including cancer cells, display distinctive PTPomes and oxPTPomes, revealing additional levels of complexity in the regulation of protein-tyrosine phosphorylation in normal and malignant cells.

PMID:
21884940
PMCID:
PMC3176638
DOI:
10.1016/j.cell.2011.07.020
[Indexed for MEDLINE]
Free PMC Article

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