Phosphoproteomics in cancer

被引：143

作者：

Harsha, H. C. ^{[1
]}

Pandey, Akhilesh ^{[2
,3
,4
,5
]}

机构：

[1] Inst Bioinformat, Bangalore 560066, Karnataka, India

[2] Johns Hopkins Univ, McKusick Nathans Inst Genet Med, Baltimore, MD 21205 USA

[3] Johns Hopkins Univ, Dept Biol Chem, Baltimore, MD 21205 USA

[4] Johns Hopkins Univ, Dept Pathol, Baltimore, MD 21205 USA

[5] Johns Hopkins Univ, Dept Oncol, Baltimore, MD 21205 USA

来源：

MOLECULAR ONCOLOGY | 2010年 / 4卷 / 06期

关键词：

SILAC; Protein microarrays; Phosphorylation; Signal transduction; GROWTH-FACTOR RECEPTOR; PHASE PROTEIN MICROARRAYS; TANDEM MASS-SPECTROMETRY; CHRONIC MYELOID-LEUKEMIA; AVIAN-SARCOMA VIRUS; CELL-CULTURE SILAC; GASTROINTESTINAL-STROMAL-TUMORS; CALCIUM-PHOSPHATE PRECIPITATION; TYROSINE PHOSPHORYLATION SITES; EMBRYONIC STEM-CELLS;

D O I：

10.1016/j.molonc.2010.09.004

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Reversible protein phosphorylation serves as a basis for regulating a number of cellular processes. Aberrant activation of kinase signaling pathways is commonly associated with several cancers. Recent developments in phosphoprotein/phosphopeptide enrichment strategies and quantitative mass spectrometry have resulted in robust pipelines for high-throughput characterization of phosphorylation in a global fashion. Today, it is possible to profile site-specific phosphorylation events on thousands of proteins in a single experiment. The potential of this approach is already being realized to characterize signaling pathways that govern oncogenesis. In addition, chemical proteomic strategies have been used to unravel targets of kinase inhibitors, which are otherwise difficult to characterize. This review summarizes various approaches used for analysis of the phosphoproteome in general, and protein kinases in particular, highlighting key cancer phosphoproteomic studies. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：482 / 495

页数：14

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