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

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.

journal_name

Cell

journal_title

Cell

authors

Karisch R,Fernandez M,Taylor P,Virtanen C,St-Germain JR,Jin LL,Harris IS,Mori J,Mak TW,Senis YA,Östman A,Moran MF,Neel BG

doi

10.1016/j.cell.2011.07.020

subject

Has Abstract

pub_date

2011-09-02 00:00:00

pages

826-40

issue

5

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(11)00818-X

journal_volume

146

pub_type

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