Sample preparation and analytical strategies for large-scale phosphoproteomics experiments |
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| Authors: | Evgeny Kanshin Stephen Michnick Pierre Thibault |
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| Affiliation: | 1. IRIC, Institute for Research in Immunology and Cancer, Université de Montréal, P.O. Box 6128, Station, Centre-ville, Montréal, Québec H3C 3J7, Canada;2. Department of Biochemistry, Université de Montréal, P.O. Box 6128, Station, Centre-ville, Montréal, Québec H3C 3J7, Canada;3. Department of Chemistry, Université de Montréal, P.O. Box 6128, Station, Centre-ville, Montréal, Québec H3C 3J7, Canada;1. Department of Plant Nutrition, College of Resources and Environmental Sciences, China Agricultural University, Beijing, PR China;2. Department of Environmental Sciences & Engineering, College of Resources and Environmental Sciences, China Agricultural University, Beijing, PR China;1. School of Pharmacy, East-China University of Science and Technology, Shanghai 200237, China;2. Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China;1. Key Laboratory of Analytical Chemistry for Biology and Medicine (Ministry of Education), Department of Chemistry, Wuhan University, Wuhan 430072, PR China;2. Wuhan Institute of Biotechnology, Wuhan 430072, PR China;1. Liaoning Provincial Key Laboratory for Proteomics, Dalian Medical University, Dalian 116044, China;2. Key Laboratory of Separation Sciences for Analytical Chemistry, National Chromatographic R. & A. Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China;1. Division of Analytical Chemistry, Institute of Chemical Sciences, Bahauddin Zakariya University, Multan 60800, Pakistan;2. Institute of Analytical Chemistry and Radiochemistry, Leopold-Franzens University, Innrain 80-82, A-6020 Innsbruck, Austria;1. Department of Chemistry, Fudan University, Shanghai 200433, China;2. Department of Chemistry, The Fifth People''s Hospital of Shanghai, Institutes of Biomedical Sciences, Collaborative Innovation Center of Genetics and Development, Fudan University, 220 Handan Road, Yangpu District, Shanghai 200433, China |
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| Abstract: | Reversible protein phosphorylation is an important post-translational modification that controls a wide range of protein functions including enzyme activity, subcellular localisation, protein degradation, intra- and inter-molecular protein interactions. Significant advances in both phosphopeptide enrichment methods and sensitive mass spectrometry instrumentation have been achieved over the past decade to facilitate the large-scale identification of protein phosphorylation in humans and different animal and microbial model systems. While mass spectrometry provides the ability to identify thousands of phosphorylation sites in a single experiment, the further understanding of the functional significance of this modification on protein substrates requires detailed information on the changes in phosphorylation stoichiometry and protein abundance across experimental paradigms. This review presents different sample preparation methods and analytical strategies used in mass spectrometry-based phosphoproteomics to profile protein phosphorylation and unravel the regulation of this modification on protein function. |
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