TY - JOUR
T1 - Advances in characterizing ubiquitylation sites by mass spectrometry
AU - Sylvestersen, K.B.
AU - Young, C.
AU - Nielsen, M.L.
PY - 2013/2
Y1 - 2013/2
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84875252687&partnerID=8YFLogxK
U2 - 10.1016/j.cbpa.2012.12.009
DO - 10.1016/j.cbpa.2012.12.009
M3 - Journal article
AN - SCOPUS:84875252687
SN - 1367-5931
VL - 17
SP - 49
EP - 58
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
IS - 1
ER -