Phosphoproteomics for the Masses

TitlePhosphoproteomics for the Masses
Publication TypeJournal Article
Year of Publication2010
AuthorsGrimsrud, PA, Swaney, DL, Wenger, CD, Beauchene, NA, Coon, JJ
JournalACS Chemical Biology
Volume5
Pagination105-119
Date PublishedJan
Type of ArticleReview
ISBN Number1554-8929
Accession NumberISI:000273653800008
KeywordsCollisional dissociation, Electron-based dissociation, electron-transfer dissociation, embryonic stem-cells, enrichment, False discovery rate, in-vivo, ion affinity-chromatography, isobaric tagging, Isotope labeling, Phosphopeptide, phosphopeptide enrichment, Phosphoproteomics, phosphorylation, Protein phosphorylation, protein-sequence analysis, quantitative phosphoproteomics, reagents, saccharomyces-cerevisiae, Shotgun proteomics, site-specific
Abstract

Protein phosphorylation serves as a primary mechanism of signal transduction in the cells of biological organisms. Technical advancements over the last several years in mass spectrometry now allow for the large-scale identification and quantitation of in vivo phosphorylation at unprecedented levels. These developments have occurred in the areas of sample preparation, instrumentation, quantitative methodology, and informatics so that today, 10 000-20 000 phosphorylation sites can be identified and quantified within a few weeks. With the rapid development and widespread availability of such data, its translation into biological insight and knowledge is a current obstacle. Here we present an overview of how this technology came to be and is currently applied, as well as future challenges for the field.

Short TitleACS Chem. Biol.