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  Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications

Doll, S., & Burlingame, A. L. (2015). Mass Spectrometry-Based Detection and Assignment of Protein Posttranslational Modifications. ACS CHEMICAL BIOLOGY, 10(1), 63-71. doi:10.1021/cb500904b.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-6D68-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-6D69-5
Genre: Journal Article

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 Creators:
Doll, Sophia1, Author              
Burlingame, Alma L.2, Author
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
2external, ou_persistent22              

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Free keywords: ELECTRON-TRANSFER DISSOCIATION; LARGE-SCALE PHOSPHOPROTEOMICS; O-GLCNACYLATION; SIGNALING NETWORKS; PROTEOMIC ANALYSIS; CAPTURE DISSOCIATION; PROTONATED PEPTIDES; CROSS-TALK; IN-VIVO; PHOSPHORYLATION
 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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Language(s): eng - English
 Dates: 2015-01
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000348332100006
DOI: 10.1021/cb500904b
 Degree: -

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Title: ACS CHEMICAL BIOLOGY
Source Genre: Journal
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Publ. Info: 1155 16TH ST, NW, WASHINGTON, DC 20036 USA : AMER CHEMICAL SOC
Pages: - Volume / Issue: 10 (1) Sequence Number: - Start / End Page: 63 - 71 Identifier: ISSN: 1554-8929