The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex
Open accessAbstract
A close-up view of the retrotranslocon: Misfolded endoplasmic reticulum (ER) proteins are retrotranslocated into the cytosol, polyubiquitinated, and degraded by the proteasome in a process known as ER-associated protein degradation (ERAD). ERAD of misfolded luminal ER proteins (ERAD-L) is mediated by the Hrd1 complex, composed of the ubiquitin ligase Hrd1 and four additional proteins (Hrd3, Der1, Usa1, and Yos9). Wu et al. report a cryo–electron microscopy structure of the active Hrd1 complex from yeast and, based on this structure, developed a model for how substrates are recognized and retrotranslocated. They propose that Hrd3 and Yos9 jointly create a luminal binding site for misfolded glycoproteins. Hrd1 and Der1 form “half-channels” juxtaposed in a thinned section of the ER membrane, which allows a polypeptide loop of an ERAD-L substrate to move through it. Science , this issue p. eaaz2449
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Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation
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Large-scale determination of previously unsolved protein structures using evolutionary information
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Self-citationStructural and molecular mechanisms for membrane protein biogenesis by the Oxa1 superfamily.
McDowell, M. A., Heimes, M., & Sinning, I. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00567-9 · Cited by 66
Molecular pathway of mitochondrial preprotein import through the TOM–TIM23 supercomplex
Zhou, X., Yang, Y., Wang, G., Wang, S., Sun, D., Ou, X., Lian, Y., & Li, L. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01103-7 · Cited by 72
Molecular view of ER membrane remodeling by the Sec61/TRAP translocon
Karki, S., Javanainen, M., Rehan, S., Tranter, D., Kellosalo, J., Huiskonen, J. T., Happonen, L., & Paavilainen, V. (2023) · The EMBO Reports · doi:10.15252/embr.202357910 · Cited by 25
Metadata
- Authors
- Wu, X., Siggel, M., Ovchinnikov, S., Mi, W., Svetlov, V., Nudler, E., Liao, M., Hummer, G., & Rapoport, T. A.
- Venue
- Science
- Published
- 2020-04-24
- Volume
- 368
- Issue
- 6489
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W3020597141
- Cited by
- 233
- References
- 6
- FWCI
- 13.42
- Type
- journal article
- Language
- en
- Open access
- green
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