A little sugar goes a long way: the cell biology of O-GlcNAc.

A little sugar goes a long way: the cell biology of O-GlcNAc.
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DOI:
10.1083/jcb.201501101
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发表时间:
2015-03-30
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Hanover JA
Hanover JA
中科院分区:
其他
文献类型:
--
作者:
Bond MR;Hanover JA

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与装饰细胞表面的复杂聚糖不同,O-连接的β-N-乙酰葡糖胺(O-GlcNAc)修饰是一种简单的细胞内Ser/Thr连接的单糖,对于疾病相关信号传导和酶调节很重要。O-GlcNAc化需要尿苷二磷酸-GlcNAc,这是一种对营养状态和其他环境线索有反应的前体。编码O-GlcNAc循环酶O-GlcNAc转移酶(OGT)和O-GlcNAc酶(OGA)的基因的选择性剪接产生靶向细胞核、细胞质和线粒体中离散位点的同种型。OGT和OGA还与细胞效应物合作,并与其他翻译后修饰协同作用。O-GlcNAc循环的酶优先作用于靶蛋白的内在无序结构域,影响转录、代谢、凋亡、细胞器生物发生和转运。
Unlike the complex glycans decorating the cell surface, the O-linked β-N-acetyl glucosamine (O-GlcNAc) modification is a simple intracellular Ser/Thr-linked monosaccharide that is important for disease-relevant signaling and enzyme regulation. O-GlcNAcylation requires uridine diphosphate–GlcNAc, a precursor responsive to nutrient status and other environmental cues. Alternative splicing of the genes encoding the O-GlcNAc cycling enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) yields isoforms targeted to discrete sites in the nucleus, cytoplasm, and mitochondria. OGT and OGA also partner with cellular effectors and act in tandem with other posttranslational modifications. The enzymes of O-GlcNAc cycling act preferentially on intrinsically disordered domains of target proteins impacting transcription, metabolism, apoptosis, organelle biogenesis, and transport.
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