钙连接蛋白在脂质双分子层中呈现出无糖的特性。

Calnexin reveals a sugar-free taste within the lipid bilayer.

作者信息

Guay Kevin P, Williams Robert V, Hebert Daniel N

机构信息

Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA, USA.

Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA, USA.

出版信息

EMBO J. 2022 Dec 15;41(24):e113003. doi: 10.15252/embj.2022113003. Epub 2022 Nov 15.

DOI:10.15252/embj.2022113003

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9753440/

Abstract

Maturation of membrane proteins is complicated by the need to fold in three distinct environments. While much is known about folding in the two aqueous milieus constituted by cytoplasm and ER lumen, our knowledge of the folding, arrangement, and quality control of transmembrane regions within the lipid bilayer, and its facilitation by molecular chaperones, is limited. New work by Bloemeke et al now reveals an expanded role of the ER chaperone calnexin acting within the lipid bilayer in a carbohydrate-independent manner.

摘要

膜蛋白的成熟因需要在三种不同环境中折叠而变得复杂。虽然我们对在由细胞质和内质网腔构成的两种水性环境中的折叠了解很多，但我们对脂质双层内跨膜区域的折叠、排列和质量控制及其由分子伴侣促进的了解有限。布洛梅克等人的新研究现在揭示了内质网伴侣钙连蛋白在脂质双层内以不依赖碳水化合物的方式发挥的扩展作用。

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