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Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications

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Doll, Sophia, Burlingame, Alma L.·2015·ACS Chemical Biology

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Abstract

Recent advances in mass spectrometry (MS)-based proteomics allow the identification and quantitation of thousands of posttranslational modification (PTM) sites in a single experiment. This follows from the development of more effective class enrichment strategies, new high performance instrumentation and bioinformatic algorithms with rigorous scoring strategies. More widespread use of these combined capabilities have led to a vast expansion in our knowledge of the complexity of biological processes mediated by PTMs. The classes most actively pursued include phosphorylation, ubiquitination, O-GlcNAcylation, methylation, and acetylation. Very recently succinylation, SUMOylation, and citrullination have emerged. Among the some 260 000 PTM sites that have been identified in the human proteome thus far, only a few have been assigned to key regulatory and/or other biological roles. Here, we provide an update of MS-based PTM analyses, with a focus on current enrichment strategies coupled with revolutionary advances in high performance MS. Furthermore, we discuss examples of the discovery of recently described biological roles of PTMs and address the challenges of defining site-specific functions.

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See all 261

Authors: Doll, S., & Burlingame, A. L.
Venue: ACS Chemical Biology
Publisher: American Chemical Society (ACS)
Published: 2014-12-26
Volume: 10
Issue: 1
Pages: 63-71
ISSN: 1554-8929 (ISSN-L)
1554-8937
DOI: 10.1021/cb500904b
OpenAlex: W2013743510
Cited by: 261
References: 93
FWCI: 6.12
Type: journal article
Language: en
Open access: hybrid

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Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications

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