O-GlcNAc Peptide Epoxyketones Are Recognized by Mammalian Proteasomes

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 pr...

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Published inJournal of the American Chemical Society Vol. 131; no. 34; pp. 12064 - 12065
Main Authors Witte, Martin D, Florea, Bogdan I, Verdoes, Martijn, Adeyanju, Oloruntosin, Van der Marel, Gijs A, Overkleeft, Herman S
Format Journal Article
LanguageEnglish
Published WASHINGTON American Chemical Society 02.09.2009
Amer Chemical Soc
Subjects
Acetylglucosamine - metabolism
Animals
Cell Line
Chemistry
Chemistry, Multidisciplinary
Humans
Ketones - metabolism
Physical Sciences
Protease Inhibitors - chemistry
Protease Inhibitors - metabolism
Protease Inhibitors - pharmacology
Proteasome Endopeptidase Complex - metabolism
Proteasome Inhibitors
Protein Binding
Science & Technology
Staining and Labeling
MHC CLASS-I
YEAST
POTENT
MOLECULES IN-VIVO
GLYCOSYLATION
INHIBITOR
EPOXOMICIN
PROTEINS
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0002-7863
1520-5126
1520-5126
DOI:10.1021/ja901231w