Post-translational modification by O-GlcNAc: another way to change protein function.
Modification of intracellular proteins by the beta-linkage of the monosaccharide, N-acetylglucosamine to serine or threonine hydroxyls (O-GlcNAc) is abundant and reversible. Although many proteins bear this post-translational covalent modification, the changes in function of the proteins as a result of this modification are only starting to be understood. In this article, we describe how aspects of the flux from the glucose backbone to this modification are modified and how the cellular activity and content of the GC-box binding transcription factor, Sp1, is altered by O-glycosylation. The association of the enzyme that puts on the O-GlcNAc modification with the bi-functional enzyme that removes this modification is discussed relative to the transition between transcriptional repression and activation.
Kudlow
Jeffrey E
JE
Department of Medicine, Division of Endocrinology, Diabetes and Metabolism, University of Alabama at Birmingham, Birmingham, AL 35294, USA. kudlow@uab.edu
D000117:Acetylglucosamine / Q000276:immunology / Q000378:metabolism*; D000818:Animals; D017209:Apoptosis; D005973:Glutamine / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D009005:Monosaccharides / Q000276:immunology / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011960:Receptors, Estrogen / Q000378:metabolism; D015398:Signal Transduction; D016329:Sp1 Transcription Factor / Q000378:metabolism; D013311:Streptozocin / Q000494:pharmacology; D000637:Transaminases / Q000037:antagonists & inhibitors / Q000378:metabolism; D014158:Transcription, Genetic / Q000235:genetics
D006023:Glycoproteins; D009005:Monosaccharides; D011960:Receptors, Estrogen; D016329:Sp1 Transcription Factor; D005973:Glutamine; D013311:Streptozocin; D000637:Transaminases; D046988:Proteasome Endopeptidase Complex; D000117:Acetylglucosamine