WFRF:(Happonen Juha Matti)
Sökning: WFRF:(Happonen Juha Matti) > Molecular view of E...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03017naa a2200421 4500 | |
| 001 | oai:lup.lub.lu.se:61196607-b460-4006-9a95-06af561bc233 | |
| 003 | SwePub | |
| 008 | 231128s2023 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://lup.lub.lu.se/record/61196607-b460-4006-9a95-06af561bc2332 URI |
| 024 | 7 | a https://doi.org/10.15252/embr.2023579102 DOI |
| 040 | a (SwePub)lu | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a art2 swepub-publicationtype |
| 072 | 7 | a ref2 swepub-contenttype |
| 100 | 1 | a Karki, Sudeepu University of Helsinki4 aut |
| 245 | 1 0 | a Molecular view of ER membrane remodeling by the Sec61/TRAP translocon |
| 264 | 1 | c 2023 |
| 520 | a Protein translocation across the endoplasmic reticulum (ER) membrane is an essential step during protein entry into the secretory pathway. The conserved Sec61 protein-conducting channel facilitates polypeptide translocation and coordinates cotranslational polypeptide-processing events. In cells, the majority of Sec61 is stably associated with a heterotetrameric membrane protein complex, the translocon-associated protein complex (TRAP), yet the mechanism by which TRAP assists in polypeptide translocation remains unknown. Here, we present the structure of the core Sec61/TRAP complex bound to a mammalian ribosome by cryogenic electron microscopy (cryo-EM). Ribosome interactions anchor the Sec61/TRAP complex in a conformation that renders the ER membrane locally thinner by significantly curving its lumenal leaflet. We propose that TRAP stabilizes the ribosome exit tunnel to assist nascent polypeptide insertion through Sec61 and provides a ratcheting mechanism into the ER lumen mediated by direct polypeptide interactions. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
| 653 | a cryo-EM | |
| 653 | a membrane proteins | |
| 653 | a protein translocation | |
| 653 | a secretory proteins | |
| 653 | a structural biology | |
| 700 | 1 | a Javanainen, Mattiu University of Helsinki4 aut |
| 700 | 1 | a Rehan, Shahidu OMass Therapeutics,University of Helsinki4 aut |
| 700 | 1 | a Tranter, Daleu University of Helsinki4 aut |
| 700 | 1 | a Kellosalo, Juhou University of Helsinki4 aut |
| 700 | 1 | a Huiskonen, Juhau University of Helsinki4 aut |
| 700 | 1 | a Happonen, Lottau Lund University,Lunds universitet,BioMS,Forskargrupper vid Lunds universitet,Strukturell infektionsmedicin,Lund University Research Groups,Structural Infection Medicine (STRIME)4 aut0 (Swepub:lu)immu-loh |
| 700 | 1 | a Paavilainen, Villeu University of Helsinki4 aut |
| 710 | 2 | a University of Helsinkib OMass Therapeutics4 org |
| 773 | 0 | t EMBO Reportsg 24:12q 24:12x 1469-221X |
| 856 | 4 | u http://dx.doi.org/10.15252/embr.202357910x freey FULLTEXT |
| 856 | 4 8 | u https://lup.lub.lu.se/record/61196607-b460-4006-9a95-06af561bc233 |
| 856 | 4 8 | u https://doi.org/10.15252/embr.202357910 |
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