Diverse regulation of protein function by O-GlcNAc: a nuclear and cytoplasmic carbohydrate post-translational modification.
N-Acetylglucosamine O-linked to serines and threonines of cytosolic and nuclear proteins (O-GlcNAc) is an abundant reversible post-translational modification found in all higher eukaryotes. Evidence for functional regulation of proteins by this dynamic saccharide is rapidly accumulating. Deletion of the gene encoding the enzyme that attaches O-GlcNAc (OGT) is lethal at the single cell level, indicating the fundamental requirement for this modification. Recent studies demonstrate a role for O-GlcNAcylation in processes as diverse as transcription in the nucleus and signaling in the cytoplasm, suggesting that O-GlcNAc has both protein and site-specific influences on biochemistry and metabolism throughout the cell.
Vosseller
Keith
K
Johns Hopkins University School of Medicine, Department of Biological Chemistry, Baltimore, MD 21218, USA.
Sakabe
Kaoru
K
Wells
Lance
L
Hart
Gerald W
GW
D000117:Acetylglucosamine / Q000378:metabolism*; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D003593:Cytoplasm / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism; D006801:Humans; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction
D009687:Nuclear Proteins; D017351:N-Acetylglucosaminyltransferases; D005947:Glucose; D000117:Acetylglucosamine