Phosphoprotein analysis: from proteins to proteomes

Frédéric Delom¹^,2 and Eric Chevet¹^,2^,3^,4

¹Dept of Surgery, McGill University, Montreal, Quebec, Canada

²Montreal Proteomics Network, McGill University, Montreal, Quebec, Canada

³Dept of Medicine, McGill University, Montreal, Quebec, Canada

⁴Dept of Anatomy, McGill University, Montreal, Quebec, Canada

author email corresponding author email

Proteome Science 2006, 4:15doi:10.1186/1477-5956-4-15


Published:	19 July 2006

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.