title: O-GlcNAc peptide epoxyketones are recognized by mammalian proteasomes.
abstract: Cytosolic and nuclear proteins may be subject to both O-GlcNAcylation and proteasomal degradation. By means of activity-based profiling, we demonstrate that O-GlcNAc serine-containing peptide epoxyketones bind to the proteasome catalytic active sites and thus provide the first clear evidence that proteasomes recognize peptides post-translationally modified with a GlcNAc moiety.
authors: Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands.
authors: Martin D
authors: MD
authors: Witte
authors: Bogdan I
authors: BI
authors: Florea
authors: Martijn
authors: M
authors: Verdoes
authors: Oloruntosin
authors: O
authors: Adeyanju
authors: Gijs A
authors: GA
authors: Van der Marel
authors: Herman S
authors: HS
authors: Overkleeft
mesh_terms: D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D006801:Humans; D007659:Ketones / Q000378:metabolism*; D011480:Protease Inhibitors / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D061988:Proteasome Inhibitors; D011485:Protein Binding; D013194:Staining and Labeling
chemical_list: D007659:Ketones; D011480:Protease Inhibitors; D061988:Proteasome Inhibitors; D046988:Proteasome Endopeptidase Complex; D000117:Acetylglucosamine