The DOI matches its Crossref record; 68 of the 68 references it cites were found in a registry or an index.
Molecular Chaperones in the Yeast Endoplasmic Reticulum Maintain the Solubility of Proteins for Retrotranslocation and Degradation
Open accessAbstract
Endoplasmic reticulum (ER)-associated degradation (ERAD) is the process by which aberrant proteins in the ER lumen are exported back to the cytosol and degraded by the proteasome. Although ER molecular chaperones are required for ERAD, their specific role(s) in this process have been ill defined. To understand how one group of interacting lumenal chaperones facilitates ERAD, the fates of pro–α-factor and a mutant form of carboxypeptidase Y were examined both in vivo and in vitro. We found that these ERAD substrates are stabilized and aggregate in the ER at elevated temperatures when BiP, the lumenal Hsp70 molecular chaperone, is mutated, or when the genes encoding the J domain–containing proteins Jem1p and Scj1p are deleted. In contrast, deletion of JEM1 and SCJ1 had little effect on the ERAD of a membrane protein. These results suggest that one role of the BiP, Jem1p, and Scj1p chaperones is to maintain lumenal ERAD substrates in a retrotranslocation-competent state.
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Cited by
One step at a time: endoplasmic reticulum-associated degradation
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A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
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Zinc transporters and the cellular trafficking of zinc
Eide, D. J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.03.005 · Cited by 874
Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
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Metadata
- Authors
- Nishikawa, S.-I., Fewell, S. W., Kato, Y., Brodsky, J. L., & Endo, T.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2001-05-28
- Volume
- 153
- Issue
- 5
- Pages
- 1061-1070
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2000806214
- Cited by
- 330
- References
- 68
- FWCI
- 6.51
- Type
- journal article
- Language
- en
- Open access
- green
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- Nishikawa, S.-I., Fewell, S. W., Kato, Y., Brodsky, J. L., & Endo, T. (2001). Molecular Chaperones in the Yeast Endoplasmic Reticulum Maintain the Solubility of Proteins for Retrotranslocation and Degradation. The Journal of Cell Biology. https://doi.org/10.1083/jcb.153.5.1061
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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