Advances in characterizing ubiquitylation sites by mass spectrometry

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

Research output: Contribution to journalJournal articleResearchpeer-review

50 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 languageEnglish
JournalCurrent Opinion in Chemical Biology
Volume17
Issue number1
Pages (from-to)49-58
Number of pages10
ISSN1367-5931
DOIs
Publication statusPublished - 5 Jan 2013

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