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The Coming of Age of Phosphoproteomics--from Large Data Sets to Inference of Protein Functions.

Roux PP, Thibault P

Institute for Research in Immunology and Cancer, Université de Montréal, P.O. Box 6128, Station. Centre-ville, Montréal, Québec H3C 3J7, Canada;

Protein phosphorylation is one of the most common post-translational modifications used in signal transduction to control cell growth, proliferation, and survival in response to both intracellular and extracellular stimuli. This modification is finely coordinated by a network of kinases and phosphatases that recognize unique sequence motifs and/or mediate their functions through scaffold and adaptor proteins. Detailed information on the nature of kinase substrates and site-specific phosphoregulation is required in order for one to better understand their pathophysiological roles. Recent advances in affinity chromatography and mass spectrometry (MS) sensitivity have enabled the large-scale identification and profiling of protein phosphorylation, but appropriate follow-up experiments are required in order to ascertain the functional significance of identified phosphorylation sites. In this review, we present meaningful technical details for MS-based phosphoproteomic analyses and describe important considerations for the selection of model systems and the functional characterization of identified phosphorylation sites.

Mol. Cell Proteomics 2013;12(12):3453-64.

Pubmed ID: 24037665

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