ArticleThe Journal of biological chemistry2012
Structural and biochemical basis of Yos9 protein dimerization and possible contribution to self-association of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation ubiquitin-ligase complex.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023Review
- Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex.Science (New York, N.Y.) · 2020Article
- Structural investigation of glycan recognition by the ERAD quality control lectin Yos9.Journal of biomolecular NMR · 2018Article
- Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway.Scientific reports · 2016Article
- Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum.Molecules (Basel, Switzerland) · 2015Review
- Glucosidase II and MRH-domain containing proteins in the secretory pathway.Current protein & peptide science · 2015Review
- Characterization of the Grp94/OS-9 chaperone-lectin complex.Journal of molecular biology · 2014Article
- Misfolded proteins induce aggregation of the lectin Yos9.The Journal of biological chemistry · 2014Article
- Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis.Trends in biochemical sciences · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In yeast, the membrane-bound HMG-CoA reductase degradation (HRD) ubiquitin-ligase complex is a key player of the ER-associated protein degradation pathway that targets misfolded proteins for proteolysis. Yos9, a component of the luminal submodule of the ligase, scans proteins for specific oligosaccharide modifications, which constitute a critical determinant of the degradation signal. Here, we report the crystal structure of the Yos9 domain that was previously suggested to confer binding to Hrd3, another component of the HRD complex. We observe an αβ-roll domain architecture and a dimeric assembly which are confirmed by analytical ultracentrifugation of both the crystallized domain and full-length Yos9. Our binding studies indicate that, instead of this domain, the N-terminal part of Yos9 including the mannose 6-phosphate receptor homology domain mediates the association with Hrd3 in vitro. Our results support the model of a dimeric state of the HRD complex and provide first-time evidence of self-association on its luminal side.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.