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- W3173722791 abstract "In eukaryotes, membrane protein folding is facilitated by a protein-conducting channel, formed by the ribosome and Sec61 translocon complex (RTC) that selectively partitions nascent peptide domains into the cytosol, ER-lumen and lipid bilayer. As a result, minor sequence variations in closely related proteins can result in markedly different folding pathways. For example, the AQP4 water channel acquires its 6-spanning topology cotranslationally as the nascent chain emerges from the ribosome, whereas AQP1 acquires an identical 6-spanning topology via topological reorientation of a transient, 4-spanning folding intermediate. Further analysis has revealed that the RTC coordinates topogenesis via sequential energetic transitions of transmembrane (TM) segments that include: insertion into Sec61α, nascent chain accumulation within the RTC, controlled TM inversion, and stable translocation of flanking residues. Progression through each of these stages is tightly coupled to chain length and involves abrupt changes in the molecular environment of the TM. Moreover, TM inversion is influenced by reversible interactions between the ribosome and a large translocon complex comprised of Sec61, TRAP and oligosaccharyltransferase. Thus the RTC facilitates membrane protein folding in a dynamic proteinaceous environment that transiently restricts nascent chain access to cytosolic and lumenal compartments." @default.
- W3173722791 created "2021-07-05" @default.
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- W3173722791 date "2011-04-01" @default.
- W3173722791 modified "2023-09-25" @default.
- W3173722791 title "Cellular mechanisms of membrane protein folding" @default.
- W3173722791 doi "https://doi.org/10.1096/fasebj.25.1_supplement.194.2" @default.
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