期刊
CURRENT OPINION IN CHEMICAL BIOLOGY
卷 53, 期 -, 页码 131-144出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.cbpa.2019.09.001
关键词
Glycosyltransferase; Glycosidase; Glycoprotein; O-GlcNAc; glycosylation; O-GlcNAcylation; Transcription; miRNA; Post-translational modification; Enzyme regulation; GIcNAc; Hexosamine; Subcellular localization; Glycans; Spliceoforms; Post-transcriptional regulation; Retained intron
资金
- Canadian Institutes of Health Research (CIHR) [PJT-148732, PJT-156202]
- Natural Sciences and Engineering Council of Canada [RGPIN298406]
- CIHR
- Michael Smith Foundation for Health Research (MSFHR)
- Biotechnology and Biological Sciences Research Council [BBSRC BB/M011151/1]
- BBSRC [1644614] Funding Source: UKRI
The post-translational modification of proteins by O-linked N-acetylglucosamine (O-GlcNAc) dynamically programmes cellular physiology to maintain homoeostasis and tailor biochemical pathways to meet context-dependent cellular needs. Despite diverse roles of played by O-GlcNAc, only two enzymes act antagonistically to govern its cycling; O-GlcNAc transferase installs the monosaccharide on target proteins, and O-GlcNAc hydrolase removes it. The recent literature has exposed a network of mechanisms regulating these two enzymes to choreograph global, and target-specific, O-GlcNAc cycling in response to cellular stress and nutrient availability. Herein, we amalgamate these emerging mechanisms from a structural and molecular perspective to explore how the cell exerts fine control to regulate O-GIcNAcylation of diverse proteins in a selective fashion.
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