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Technologies and challenges in large‐scale phosphoproteomics
Author(s) -
EngholmKeller Kasper,
Larsen Martin R.
Publication year - 2013
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201200484
Subject(s) - phosphoproteomics , phosphorylation , protein phosphorylation , proteomics , computational biology , biology , microbiology and biotechnology , biochemistry , protein kinase a , gene
Phosphorylation, the reversible addition of a phosphate group to amino acid side chains of proteins, is a fundamental regulator of protein activity, stability, and molecular interactions. Most cellular processes, such as inter‐ and intracellular signaling, protein synthesis, degradation, and apoptosis, rely on phosphorylation. This PTM is thus involved in many diseases, rendering localization and assessment of extent of phosphorylation of major scientific interest. MS ‐based phosphoproteomics, which aims at describing all phosphorylation sites in a specific type of cell, tissue, or organism, has become the main technique for discovery and characterization of phosphoproteins in a nonhypothesis driven fashion. In this review, we describe methods for state‐of‐the‐art MS ‐based analysis of protein phosphorylation as well as the strategies employed in large‐scale phosphoproteomic experiments with focus on the various challenges and limitations this field currently faces.