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|Title:||Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation.|
Savitski, Mikhail M.
|Publisher:||Public Library of Science|
|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|
|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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