Please use this identifier to cite or link to this item: doi:10.22028/D291-27893
Title: Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation.
Authors: Pereira, Fabio
Rettel, Mandy
Stein, Frank
Savitski, Mikhail M.
Collinson, Ian
Römisch, Karin
Language: English
Title: PLOS ONE
Volume: 14
Book: 1
Pages: e0211180
Publisher: Public Library of Science
Issue Date: 2019
DDC groups: 570 Life sciences, biology
Publikation type: Journal Article
Abstract: Proteins that misfold in the endoplasmic reticulum (ER) are transported back to the cytosol for ER-associated degradation (ERAD). The Sec61 channel is one of the candidates for the retrograde transport conduit. Channel opening from the ER lumen must be triggered by ERAD factors and substrates. Here we aimed to identify new lumenal interaction partners of the Sec61 channel by chemical crosslinking and mass spectrometry. In addition to known Sec61 interactors we detected ERAD factors including Cue1, Ubc6, Ubc7, Asi3, and Mpd1. We show that the CPY* ERAD factor Mpd1 binds to the lumenal Sec61 hinge region. Deletion of the Mpd1 binding site reduced the interaction between both proteins and caused an ERAD defect specific for CPY* without affecting protein import into the ER or ERAD of other substrates. Our data suggest that Mpd1 binding to Sec61 is a prerequisite for CPY* ERAD and confirm a role of Sec61 in ERAD of misfolded secretory proteins.
DOI of the first publication: 10.1371/journal.pone.0211180
URI: urn:nbn:de:bsz:291--ds-278933
hdl:20.500.11880/27394
http://dx.doi.org/10.22028/D291-27893
ISSN: 1932-6203
Date issued: 11-Apr-2019
Third-party funds sponsorship: IC received funding from the BBSRC
Sponsorship ID: BB/M003604/1 and BB/N015126/1
Notes: We acknowledge support by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) and Saarland University within the funding programme Open Access Publishing.
Faculty: NT - Naturwissenschaftlich- Technische Fakultät
Institute: NT - Biowissenschaften
Appears in Collections:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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