期刊
FRONTIERS IN ENDOCRINOLOGY
卷 5, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fendo.2014.00183
关键词
O-GIcNAcylation; O-GIcNAc transferase; O-GIcNAcase; signaling; transcription; diabetes; cancer; Alzheimer's disease
资金
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL107153] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [P30DK079637] Funding Source: NIH RePORTER
- NHLBI NIH HHS [P01 HL107153] Funding Source: Medline
- NIDDK NIH HHS [P30 DK079637] Funding Source: Medline
Even though the dynamic modification of polypeptides by the monosaccharide, O-linked N-acetylglucosamine (O-GIcNAcylation) was discovered over 30 years ago, its physiological significance as a major nutrient sensor that regulates myriad cellular processes has only recently been more widely appreciated. O-GIcNAcylation, either on its own or by its interplay with other post-translational modifications, such as phosphorylation, ubiquitination, and others, modulates the activities of signaling proteins, regulates most components of the transcription machinery, affects cell cycle progression and regulates the targeting/turnover or functions of myriad other regulatory proteins, in response to nutrients. Acute increases in O-GIcNAcylation protect cells from stress-induced injury, while chronic deregulation of O-GIcNAc cycling contributes to the etiology of major human diseases of aging, such as diabetes, cancer, and neurodegeneration. Recent advances in tools to study O-GIcNAcylation at the individual site level and specific inhibitors of O-GIcNAc cycling have allowed more rapid progress toward elucidating the specific functions of OIcNAcylation in essential cellular processes.
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