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
Celljournal_title
Cellauthors
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 BGdoi
10.1016/j.cell.2011.07.020subject
Has Abstractpub_date
2011-09-02 00:00:00pages
826-40issue
5eissn
0092-8674issn
1097-4172pii
S0092-8674(11)00818-Xjournal_volume
146pub_type
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