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Curr Opin Chem Biol. 2013 Feb;17(1):49-58. doi: 10.1016/j.cbpa.2012.12.009. Epub 2013 Jan 5.

Advances in characterizing ubiquitylation sites by mass spectrometry.

Author information

1
Department of Proteomics, The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health Sciences, DK-2200 Copenhagen, Denmark.

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.

PMID:
23298953
DOI:
10.1016/j.cbpa.2012.12.009
[Indexed for MEDLINE]

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