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.

中文翻译：

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钙连接蛋白在脂质双层内揭示无糖味道

由于需要在三种不同的环境中折叠，膜蛋白的成熟变得复杂。虽然我们对由细胞质和内质网腔构成的两个水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的促进的了解是有限的。Bloemeke等人的新工作现在揭示了内质网伴侣钙连接蛋白以不依赖碳水化合物的方式在脂质双层内发挥作用的扩大作用。