ArticleBMC cell biology2013
ERAD and protein import defects in a sec61 mutant lacking ER-lumenal loop 7.
Article in BMC cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Spotlight on TAP and its vital role in antigen presentation and cross-presentation.Molecular immunology · 2022Review
- Nanopore-Based Comparative Transcriptome Analysis Reveals the Potential Mechanism of High-Temperature Tolerance in Cotton (Plants (Basel, Switzerland) · 2021Article
- Review
- Toxins Utilize the Endoplasmic Reticulum-Associated Protein Degradation Pathway in Their Intoxication Process.International journal of molecular sciences · 2019Review
- Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation.PloS one · 2019Article
- Article
- Regulation of the Cell Biology of Antigen Cross-Presentation.Annual review of immunology · 2018Review
- Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.Molecular cell · 2017Article
- Sec61 blockade by mycolactone inhibits antigen cross-presentation independently of endosome-to-cytosol export.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Glycosylation-directed quality control of protein folding.Nature reviews. Molecular cell biology · 2015Review
- Article
- Hsp90 modulates PPARγ activity in a mouse model of nonalcoholic fatty liver disease.Journal of lipid research · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe Sec61 channel mediates protein translocation across the endoplasmic reticulum (ER) membrane during secretory protein biogenesis, and likely also during export of misfolded proteins for ER-associated degradation (ERAD). The mechanisms of channel opening for the different modes of translocation are not understood so far, but the position of the large ER-lumenal loop 7 of Sec61p suggests a decisive role.
resultsWe show here that the Y345H mutation in L7 which causes diabetes in the mouse displays no ER import defects in yeast, but a delay in misfolded protein export. A complete deletion of L7 in Sec61p resulted in viable, cold- and tunicamycin-hypersensitive yeast cells with strong defects in posttranslational protein import of soluble proteins into the ER, and in ERAD of soluble substrates. Membrane protein ERAD was only moderately slower in sec61∆L7 than in wildtype cells. Although Sec61∆L7 channels were unstable in detergent, co-translational protein integration into the ER membrane, proteasome binding to Sec61∆L7 channels, and formation of hetero-heptameric Sec complexes were not affected.
conclusionsWe conclude that L7 of Sec61p is required for initiation of posttranslational soluble protein import into and misfolded soluble protein export from the ER, suggesting a key role for L7 in transverse gating of the Sec61 channel.
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