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dc.contributor.authorO'Keefe, Sarah; orcid: 0000-0002-1744-0198; email: sarah.okeefe@manchester.ac.uk
dc.contributor.authorPool, Martin R.; orcid: 0000-0003-3071-1535; email: martin.r.pool@manchester.ac.uk
dc.contributor.authorHigh, Stephen; orcid: 0000-0002-4532-8152; email: stephen.high@manchester.ac.uk
dc.date.accessioned2021-06-05T11:30:10Z
dc.date.available2021-06-05T11:30:10Z
dc.date.issued2021-06-05
dc.date.submitted2021-02-18
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/624850/febs.15905.pdf?sequence=2
dc.identifierhttps://chesterrep.openrepository.com/bitstream/handle/10034/624850/febs.15905.xml?sequence=3
dc.identifier.citationThe FEBS Journal
dc.identifier.urihttp://hdl.handle.net/10034/624850
dc.descriptionFrom Wiley via Jisc Publications Router
dc.descriptionHistory: received 2021-02-18, rev-recd 2021-04-19, accepted 2021-04-28, pub-electronic 2021-06-05
dc.descriptionArticle version: VoR
dc.descriptionPublication status: Published
dc.descriptionFunder: Biochemical Society; Id: http://dx.doi.org/10.13039/501100000373
dc.descriptionFunder: Wellcome Trust; Grant(s): 204957/Z/16/Z
dc.description.abstractThe Sec61 complex is the major protein translocation channel of the endoplasmic reticulum (ER), where it plays a central role in the biogenesis of membrane and secretory proteins. Whilst Sec61‐mediated protein translocation is typically coupled to polypeptide synthesis, suggestive of significant complexity, an obvious characteristic of this core translocation machinery is its surprising simplicity. Over thirty years after its initial discovery, we now understand that the Sec61 complex is in fact the central piece of an elaborate jigsaw puzzle, which can be partly solved using new research findings. We propose that the Sec61 complex acts as a dynamic hub for co‐translational protein translocation at the ER, proactively recruiting a range of accessory complexes that enhance and regulate its function in response to different protein clients. It is now clear that the Sec61 complex does not have a monopoly on co‐translational insertion, with some transmembrane proteins preferentially utilising the ER membrane complex instead. We also have a better understanding of post‐insertion events, where at least one membrane‐embedded chaperone complex can capture the newly inserted transmembrane domains of multi‐span proteins and co‐ordinate their assembly into a native structure. Having discovered this array of Sec61‐associated components and competitors, our next challenge is to understand how they act together in order to expand the range and complexity of the membrane proteins that can be synthesised at the ER. Furthermore, this diversity of components and pathways may open up new opportunities for targeted therapeutic interventions designed to selectively modulate protein biogenesis at the ER.
dc.languageen
dc.rightsLicence for VoR version of this article: http://creativecommons.org/licenses/by/4.0/
dc.sourceissn: 1742-464X
dc.sourceissn: 1742-4658
dc.subjectState‐Of‐The‐Art Review
dc.subjectState‐Of‐The‐Art Reviews
dc.subjectco‐translational translocation
dc.subjectEMC
dc.subjectmembrane protein insertion
dc.subjectPAT complex
dc.subjectSec61
dc.subjectSec62/Sec63
dc.subjectSRP
dc.subjectTMCO1 translocon
dc.subjectTRAP complex
dc.titleMembrane protein biogenesis at the ER: the highways and byways
dc.typearticle
dc.date.updated2021-06-05T11:30:10Z
dc.date.accepted2021-04-28


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