Phosphoprotein analysis: from proteins to proteomes |
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Authors: | Frédéric Delom Eric Chevet |
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Institution: | (1) Dept of Surgery, McGill University, Montreal, Quebec, Canada;(2) Montreal Proteomics Network, McGill University, Montreal, Quebec, Canada;(3) Dept of Medicine, McGill University, Montreal, Quebec, Canada;(4) Dept of Anatomy, McGill University, Montreal, Quebec, Canada |
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Abstract: | Characterization of protein modification by phosphorylation is one of the major tasks that have to be accomplished in the
post-genomic era. Phosphorylation is a key reversible modification occurring mainly on serine, threonine and tyrosine residues
that can regulate enzymatic activity, subcellular localization, complex formation and degradation of proteins. The understanding
of the regulatory role played by phosphorylation begins with the discovery and identification of phosphoproteins and then
by determining how, where and when these phosphorylation events take place. Because phosphorylation is a dynamic process difficult
to quantify, we must at first acquire an inventory of phosphoproteins and characterize their phosphorylation sites. Several
experimental strategies can be used to explore the phosphorylation status of proteins from individual moieties to phosphoproteomes.
In this review, we will examine and catalogue how proteomics techniques can be used to answer specific questions related to
protein phosphorylation. Hence, we will discuss the different methods for enrichment of phospho-proteins and -peptides, and
then the various technologies for their identification, quantitation and validation. |
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Keywords: | |
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