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糖基化定向的蛋白质折叠质量控制。

Glycosylation-directed quality control of protein folding.

机构信息

Temasek Life Sciences Laboratory, National University of Singapore, 1 Research Link, Singapore 117604.

Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543.

出版信息

Nat Rev Mol Cell Biol. 2015 Dec;16(12):742-52. doi: 10.1038/nrm4073. Epub 2015 Oct 14.

Abstract

Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated in the endoplasmic reticulum. These adducts have many biological functions, including, notably, their contribution to the maturation of glycoproteins. N-linked glycans are of oligomeric structure, forming configurations that provide blueprints to precisely instruct the folding of protein substrates and the quality control systems that scrutinize it. O-linked mannoses are simpler in structure and were recently found to have distinct functions in protein quality control that do not require the complex structure of N-linked glycans. Together, recent studies reveal the breadth and sophistication of the roles of these glycan-directed modifications in protein biogenesis.

摘要

分泌途径中的膜结合蛋白和可溶性蛋白通常在内质网中发生糖基化。这些加合物具有许多生物学功能,包括特别地,它们对糖蛋白成熟的贡献。N 连接聚糖具有寡聚结构,形成的结构为精确指导蛋白质底物的折叠和质量控制系统提供了蓝图,该系统对其进行了检查。O 连接甘露糖在结构上更简单,最近发现它们在蛋白质质量控制中具有独特的功能,而不需要 N 连接聚糖的复杂结构。总之,最近的研究揭示了这些糖基化导向修饰在蛋白质生物发生中的广泛而复杂的作用。

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