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pubmed-article:10411645pubmed:abstractTextThe novel intracellular carbohydrate O-linked N-acetylglucosamine (O-GlcNAc) is present on proteins ranging from those of viruses to those of humans and include cytosolic, nuclear and plasma-membrane proteins. In this report we have examined the effect of manipulation of phosphorylation on the levels of O-GlcNAc in cerebellar neurons from early postnatal mice. Our results indicate a reciprocal response of O-GlcNAc levels to phosphorylation. Activation of protein kinase A or C, for example, results in reduced levels of O-GlcNAc specifically in the fraction of cytoskeletal and cytoskeleton-associated proteins, while inhibition of the same kinases results in increased levels of O-GlcNAc. These data are in keeping with a reciprocal action of O-GlcNAc with respect to phosphorylation and suggest that this modification may have a role in signal transduction.lld:pubmed
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pubmed-article:10411645pubmed:articleTitleO-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation.lld:pubmed
pubmed-article:10411645pubmed:affiliationDepartment of Biochemistry, Institute for Animal Anatomy and Physiology, University of Bonn, Germany.lld:pubmed
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pubmed-article:10411645pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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