Global Proteomic Assessment of the Classical Protein-Tyrosine Phosphatome and "Redoxome''

被引：141

作者：

Karisch, Robert ^{[1
,2
,3
]}

Fernandez, Minerva ^{[2
,3
]}

Taylor, Paul ^{[4
,5
,6
,7
]}

Virtanen, Carl ^{[2
,3
]}

St-Germain, Jonathan R. ^{[4
,5
,6
,7
]}

Jin, Lily L. ^{[4
,5
,6
,7
]}

Harris, Isaac S. ^{[2
,3
]}

Mori, Jun ^{[8
]}

Mak, Tak W. ^{[2
,3
]}

Senis, Yotis A. ^{[8
]}

Ostman, Arne ^{[9
]}

Moran, Michael F. ^{[4
,5
,6
,7
]}

Neel, Benjamin G. ^{[1
,2
,3
]}

机构：

[1] Univ Toronto, Dept Med Biophys, Toronto, ON M5G 2M9, Canada

[2] Univ Hlth Network, Campbell Family Canc Res Inst, Ontario Canc Inst, Toronto, ON M5G 1L7, Canada

[3] Univ Hlth Network, Princess Margaret Hosp, Toronto, ON M5G 1L7, Canada

[4] Univ Toronto, Program Mol Struct & Funct, Hosp Sick Children, Toronto, ON M5G 1L7, Canada

[5] Univ Toronto, Dept Mol Genet, Toronto, ON M5G 1L7, Canada

[6] Univ Toronto, McLaughlin Ctr Mol Med, Toronto, ON M5G 1L7, Canada

[7] Univ Toronto, Banting & Best Dept Med Res, Toronto, ON M5G 1L7, Canada

[8] Univ Birmingham, Ctr Cardiovasc Sci, Inst Biomed Res, Sch Clin & Expt Med,Coll Med & Dent Sci, Birmingham B15 2TT, W Midlands, England

[9] Karolinska Inst, Canc Ctr Karolinska, Dept Pathol & Oncol, S-17176 Stockholm, Sweden

来源：

CELL | 2011年 / 146卷 / 05期

基金：

美国国家卫生研究院; 加拿大健康研究院; 瑞典研究理事会;

关键词：

SPECTROMETRY-BASED PROTEOMICS; EPIDERMAL-GROWTH-FACTOR; MASS-SPECTROMETRY; REVERSIBLE OXIDATION; IN-VIVO; CANCER; CELLS; 1B; INACTIVATION; CYSTEINE;

D O I：

10.1016/j.cell.2011.07.020

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 H2O2. 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.

引用

页码：826 / 840

页数：15

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