The coming of age of phosphoproteomics--from large data sets to inference of protein functions.

  • Philippe P Roux, Pierre Thibault
  • Published 2013 in Molecular & cellular proteomics : MCP

Abstract

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.

DOI: 10.1074/mcp.R113.032862
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@article{Roux2013TheCO, title={The coming of age of phosphoproteomics--from large data sets to inference of protein functions.}, author={Philippe P Roux and Pierre Thibault}, journal={Molecular & cellular proteomics : MCP}, year={2013}, volume={12 12}, pages={3453-64} }