Mechanism of an intramembrane chaperone for multipass membrane proteins.

ABSTRACT: Multipass membrane proteins play numerous roles in biology and include receptors, transporters, ion channels and enzymes^1,2. How multipass proteins are co-translationally inserted and folded at the endoplasmic reticulum is not well understood². The prevailing model posits that each transmembrane domain (TMD) of a multipass protein successively passes into the lipid bilayer through a front-side lateral gate of the Sec61 protein translocation channel^3-9. The PAT complex, an intramembrane chaperone comprising Asterix and CCDC47, engages early TMDs of multipass proteins to promote their biogenesis by an unknown mechanism¹⁰. Here, biochemical and structural analysis of intermediates during multipass protein biogenesis showed that the nascent chain is

SUBMITTER: Smalinskaite L 

PROVIDER: S-EPMC7614104 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature