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


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.

SUBMITTER: Guay KP 

PROVIDER: S-EPMC9753440 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature

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

Guay Kevin P KP   Williams Robert V RV   Hebert Daniel N DN  

The EMBO journal 20221115 24


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 carbohy  ...[more]

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