title: Advances in characterizing ubiquitylation sites by mass spectrometry.
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.
authors.affiliation: Department of Proteomics, The Novo Nordisk Foundation Center for Protein Research, University of Copenhagen, Faculty of Health Sciences, DK-2200 Copenhagen, Denmark.
authors.forename: Kathrine B
authors.initials: KB
authors.lastname: Sylvestersen
authors.forename: Clifford
authors.initials: C
authors.lastname: Young
authors.forename: Michael L
authors.initials: ML
authors.lastname: Nielsen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism*; D057149:Ubiquitinated Proteins / Q000737:chemistry / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D025801:Ubiquitin; D057149:Ubiquitinated Proteins