Advances in characterizing ubiquitylation sites by mass spectrometry

K.B. Sylvestersen; C. Young; M.L. Nielsen

doi:10.1016/j.cbpa.2012.12.009

Advances in characterizing ubiquitylation sites by mass spectrometry

K.B. Sylvestersen, C. Young, M.L. Nielsen

Novo Nordisk Foundation Center for Protein Research

46 Citations (Scopus)

Abstract

The attachment of one or more ubiquitin moieties to proteins plays a central regulatory mechanism in eukaryotic cells. Protein ubiquitylation regulates numerous cellular processes, including protein degradation, signal transduction, DNA repair and cell division. The characterization of ubiquitylation is a two-fold challenge that involves the mapping of ubiquitylation sites and the determination of ubiquitin chain topology. This review focuses on the technical advances in the mass spectrometry-based characterization of ubiquitylation sites, which have recently involved the large-scale identification of ubiquitylation sites by peptide-level enrichment strategies. The discovery that ubiquitylation is a widespread modification similar to phosphorylation and acetylation suggests cross-talk may also occur at the post translational modification level.

Original language	English
Journal	Current Opinion in Chemical Biology
Volume	17
Issue number	1
Pages (from-to)	49-58
Number of pages	10
ISSN	1367-5931
DOIs	https://doi.org/10.1016/j.cbpa.2012.12.009
Publication status	Published - Feb 2013

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Advances in characterizing ubiquitylation sites by mass spectrometry

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