Phosphoproteomics in cancer

H. C. Harsha; Akhilesh Pandey

doi:10.1016/j.molonc.2010.09.004

Phosphoproteomics in cancer

H. C. Harsha, Akhilesh Pandey

School of Medicine

Research output: Contribution to journal › Article › peer-review

117 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	482-495
Number of pages	14
Journal	Molecular Oncology
Volume	4
Issue number	6
DOIs	https://doi.org/10.1016/j.molonc.2010.09.004
State	Published - Dec 2010

Keywords

Phosphorylation
Protein microarrays
Signal transduction
SILAC

ASJC Scopus subject areas

Cancer Research
Genetics
Molecular Medicine

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10.1016/j.molonc.2010.09.004

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abstract = "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.",

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Phosphoproteomics in cancer

Abstract

Keywords

ASJC Scopus subject areas

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