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Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins
Author(s) -
Temporini Caterina,
Calleri Enrica,
Massolini Gabriella,
Caccialanza Gabriele
Publication year - 2008
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.20164
Subject(s) - chemistry , glycosylation , posttranslational modification , phosphorylation , mass spectrometry , proteome , computational biology , protein phosphorylation , function (biology) , gene isoform , proteomics , biochemistry , chromatography , gene , microbiology and biotechnology , enzyme , protein kinase a , biology
The post‐translational modification (PTM) of proteins is a common biological mechanism for regulating protein localization, function, and turnover. The direct analysis of modifications is required because they are not coded by genes, and thus are not predictable. Different MS‐based proteomic strategies are used for the analysis of PTMs, such as phosphorylation and glycosylation, and are composed of a structural simplification step of the protein followed by specific isolation step to extract the classes of modified peptides (also called “sub‐proteomes”) before mass spectrometry. This specific isolation step is necessary because PTMs occur at a sub‐stoichiometric level and signal suppression of the modified fractions in the mass spectrometer occurs in the presence of the more‐abundant non‐modified counterpart. The request of innovative analytical strategies in PTM studies is the capability to localize the modification sites, give detailed structural information on the modification, and determine the isoform composition with increased selectivity, sensitivity, and throughput. This review focuses on the description of recent integrated analytical systems proposed for the analysis of PTMs in proteins, and their application to profile the glycoproteome and the phosphoproteome in biological samples. Comments on the difficulties and usefulness of the analytical strategies are given. © 2008 Wiley Periodicals, Inc. Mass Spec Rev. 27:207–236, 2008