The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate
Open accessAbstract
Until recently, the degradation of aberrant and unassembled proteins retained in the endoplasmic reticulum (ER) was thought to involve unidentified ER-localized proteases. We now show that the ER-associated degradation (ERAD) of two mutant proteins that accumulate in the ER lumen is inhibited in a proteasome-defective yeast strain and when cytosol from this mutant is used in an in vitro assay. In addition, ERAD is limited in vitro in the presence of the proteasome inhibitors, 3,4-dichloroisocoumarin and lactacystin. Furthermore, we find that an ERAD substrate is exported from ER-derived microsomes, and the accumulation of exported substrate is 2-fold greater when proteasome mutant cytosol is used in place of wild-type cytosol. We conclude that lumenal ERAD substrates are exported from the yeast ER to the cytoplasm for degradation by the proteasome complex.
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Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
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Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
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Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
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Glycosylation and the Immune System
Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A., & Dwek, R. A. (2001) · Science · doi:10.1126/science.291.5512.2370 · Cited by 1,588
One step at a time: endoplasmic reticulum-associated degradation
Vembar, S. S., & Brodsky, J. L. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2546 · Cited by 1,299
Self-citationProtein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response
Zhang, K., & Kaufman, R. J. (2005) · Handbook of Experimental Pharmacology · doi:10.1007/3-540-29717-0_3 · Cited by 152
Spiro, R. G. (2004) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-004-4037-8 · Cited by 149
Metadata
- Authors
- Werner, E. D., Brodsky, J. L., & McCracken, A. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1996-11-26
- Volume
- 93
- Issue
- 24
- Pages
- 13797-13801
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1977498240
- Cited by
- 462
- References
- 35
- FWCI
- 10.86
- Type
- journal article
- Language
- en
- Open access
- green
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- Werner, E. D., Brodsky, J. L., & McCracken, A. A. (1996). Proteasome-dependent endoplasmic reticulum-associated protein degradation: An unconventional route to a familiar fate. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.24.13797
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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).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
