O-GlcNAc cycling: Implications for neurodegenerative disorders

The dynamic post-translational modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc), termed O-GlcNAcylation, is an important mechanism for modulating cellular signaling pathways. O-GlcNAcylation impacts transcription, translation, organelle trafficking, proteasomal degradation and apo...

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Bibliographic Details
Published in:The international journal of biochemistry & cell biology 2009-11, Vol.41 (11), p.2134-2146
Main Authors: Lazarus, Brooke D., Love, Dona C., Hanover, John A.
Format: Article
Language:English
Subjects:
Acetylglucosamine - metabolism
Acetylglucosaminidase - chemistry
Acetylglucosaminidase - metabolism
Animals
Gene Expression Regulation
Glycosylation
Humans
N-Acetylglucosaminyltransferases - chemistry
N-Acetylglucosaminyltransferases - metabolism
Neurodegenerative Diseases - enzymology
Neurodegenerative Diseases - genetics
Neurodegenerative Diseases - metabolism
O-GlcNAc transferase
O-GlcNAcase
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Summary:The dynamic post-translational modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc), termed O-GlcNAcylation, is an important mechanism for modulating cellular signaling pathways. O-GlcNAcylation impacts transcription, translation, organelle trafficking, proteasomal degradation and apoptosis. O-GlcNAcylation has been implicated in the etiology of several human diseases including type-2 diabetes and neurodegeneration. This review describes the pair of enzymes responsible for the cycling of this post-translational modification: O-GlcNAc transferase (OGT) and β-N-acetylglucosaminidase (OGA), with a focus on the function of their structural domains. We will also highlight the important processes and substrates regulated by these enzymes, with an emphasis on the role of O-GlcNAc as a nutrient sensor impacting insulin signaling and the cellular stress response. Finally, we will focus attention on the many ways by which O-GlcNAc cycling may affect the cellular machinery in the neuroendocrine and central nervous systems.
ISSN:1357-2725
1878-5875
DOI:10.1016/j.biocel.2009.03.008