Protein phosphorylation is a reversible post-translational modification that is involved in virtually all eukaryotic cellular processes and has been studied in great detail in recent years. Many developments in mass spectrometry (MS)-based proteomics have been successfully applied to study protein phosphorylation in highly complicated samples. Furthermore, the emergence of a variety of enrichment strategies has allowed some of the challenges associated with low phosphorylation stoichiometry and phosphopeptide copy number to be overcome. The dynamic nature of protein phosphorylation complicates its analysis; however, a number of methods have been developed to successfully quantitate phosphorylation changes in a variety of cellular systems. The following review details some of the most recent breakthroughs in the study of protein phosphorylation, or phosphoproteomics, using MS-based approaches. The majority of the focus is placed on detailing strategies that are currently used to conduct MS-based quantitative phosphoproteomics.

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Keywords Affinity purification, Isotopic labelling, Mass spectrometry, Phosphoproteomics, Quantitation
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Journal Biochemistry and Cell Biology
Smith, J. C, & Figeys, D. (Daniel). (2008). Recent developments in mass spectrometry-based quantitative phosphoproteomics. In Biochemistry and Cell Biology (Vol. 86, pp. 137–148). doi:10.1139/O08-007