Systems-wide proteomic characterization of combinatorial post-translational modification patterns

• Published in: Expert review of proteomics Vol. 7; no. 1; pp. 79 - 92
• Main Authors: Young, Nicolas L, Plazas-Mayorca, Mariana D, Garcia, Benjamin A
• Format: Journal Article
• Language: English
• Published: England Taylor & Francis 01.02.2010; Expert Reviews Ltd; Informa Healthcare
• Subjects: electron-capture dissociation; electron-transfer dissociation; histone code; Mass spectrometry; Mass Spectrometry - methods; Methods; middle-down approach; Observations; Post-translational modification; Properties; Protein Processing, Post-Translational; Proteins - analysis; Proteomics; Proteomics - methods; top-down approach; United States
• ISSN: 1478-9450; 1744-8387
• DOI: 10.1586/epr.09.100

Protein post-translational modifications (PTMs) have been widely shown to influence protein-protein interactions, direct subcellular location and transduce a variety of both internal and externally generated signals into cellular/phenotypic outcomes. Mass spectrometry has been a key tool for the elucidation of several types of PTMs in both qualitative and quantitative manners. As large datasets on the proteome-wide level are now being generated on a daily basis, the identification of combinatorial PTM patterns has become feasible. A survey of the recent literature in this area shows that many proteins undergo multiple modifications and that sequential or hierarchal patterns exist on many proteins; the biology of these modification patterns is only starting to be unraveled. This review will outline combinatorial PTM examples in biology, and the mass spectrometry-based techniques and applications utilized in the investigations of these combinatorial PTMs.