TY - JOUR
T1 - Diverse regulation of protein function by O-GlcNAc
T2 - A nuclear and cytoplasmic carbohydrate post-translational modification
AU - Vosseller, Keith
AU - Sakabe, Kaoru
AU - Wells, Lance
AU - Hart, Gerald Warren
PY - 2002/12/1
Y1 - 2002/12/1
N2 - 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.
AB - 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.
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U2 - 10.1016/S1367-5931(02)00384-8
DO - 10.1016/S1367-5931(02)00384-8
M3 - Article
C2 - 12470741
AN - SCOPUS:0036898933
SN - 1367-5931
VL - 6
SP - 851
EP - 857
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
IS - 6
ER -