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O-连接的N-乙酰葡糖胺糖基化(O-GlcNAcylation)与表观遗传学之间潜在的协调作用。

Potential coordination role between O-GlcNAcylation and epigenetics.

作者信息

Wu Donglu, Cai Yong, Jin Jingji

机构信息

School of Life Sciences, Jilin University, Changchun, 130012, China.

National Engineering Laboratory for AIDS Vaccine, Jilin University, Changchun, 130012, China.

出版信息

Protein Cell. 2017 Oct;8(10):713-723. doi: 10.1007/s13238-017-0416-4. Epub 2017 May 9.

DOI:10.1007/s13238-017-0416-4
PMID:28488246
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5636747/
Abstract

Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells. O-GlcNAcylation often occurs on serine (Ser) and threonine (Thr) residues of the specific substrate proteins via the addition of O-GlcNAc group by OGT. It has been known that O-GlcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GlcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GlcNAcylation as 'protein code' or 'histone code' may provide recognition platforms or executive instructions for subsequent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GlcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O-GlcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GlcNAcylation with epigenetic changes in intracellular biological processes.

摘要

翻译后O-连接的β-N-乙酰葡糖胺修饰(O-GlcNAc糖基化)的动态变化在细胞中由O-连接的β-N-乙酰葡糖胺(O-GlcNAc)转移酶(OGT)和糖苷水解酶O-GlcNAcase(OGA)控制。O-GlcNAc糖基化通常通过OGT添加O-GlcNAc基团,发生在特定底物蛋白的丝氨酸(Ser)和苏氨酸(Thr)残基上。已知O-GlcNAc糖基化不仅参与许多基本的细胞过程,还通过各种机制在癌症发展中发挥重要作用。最近,越来越多的数据表明,组蛋白或非组蛋白上的O-GlcNAc糖基化可导致随后生物过程的启动,这表明O-GlcNAc糖基化作为“蛋白质密码”或“组蛋白密码”可能为随后招募蛋白质以执行特定功能提供识别平台或执行指令。在本综述中,我们总结了O-GlcNAc糖基化与表观遗传变化的相互作用,介绍了最近将O-GlcNAc糖基化与表观遗传变化之间的串扰联系起来的研究发现,并推测了O-GlcNAc糖基化在细胞内生物过程中与表观遗传变化的潜在协调作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/dff6785a8a59/13238_2017_416_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/a29afce7a56c/13238_2017_416_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/da899c25b15d/13238_2017_416_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/d7f1deaa689e/13238_2017_416_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/dff6785a8a59/13238_2017_416_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/a29afce7a56c/13238_2017_416_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/da899c25b15d/13238_2017_416_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/d7f1deaa689e/13238_2017_416_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d9b5/5636747/dff6785a8a59/13238_2017_416_Fig4_HTML.jpg

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