期刊
BRAIN RESEARCH BULLETIN
卷 133, 期 -, 页码 80-87出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.brainresbull.2016.08.002
关键词
OGT; OGA; Tau; Synuclein; Amyloid; Huntingtin; Aging; Autophagy
资金
- UAB AMC21 [HL101192, HL-110366, R01NS076312, NIHR01-NS064090]
O-GlcNAcylation is a dynamic form of protein glycosylation which involves the addition of beta-b-N-acetylglucosamine (GlcNAc) via an O-linkage to serine or threonine residues of nuclear, cytoplasmic, mitochondrial and transmembrane proteins. The two enzymes responsible for O-GIcNAc cycling are O-GlcNAc transferase (OGT) and O-GIcNAcase (OGA); their expression and activities in brain are age dependent. More than 1000 O-GlcNAc protein targets have been identified which play critical roles in many cellular processes. In mammalian brain, O-GlcNAc modification of Tau decreases its phosphorylation and toxicity, suggesting a neuroprotective role of pharmacological elevation of brain O-GlcNAc for Alzheimer's disease treatment. Other observations suggest that elevating O-GlcNAc levels may decrease protein clearance or induce apoptosis. This review highlights some of the key findings regarding O-GlcNAcylation in models of neurodegenerative diseases. (C) 2016 Elsevier Inc. All rights reserved.
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