The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Degradation of CFTR by the ubiquitin-proteasome pathway
Open accessAbstract
Most cases of cystic fibrosis are caused by mutations that interfere with the biosynthetic folding of the cystic fibrosis transmembrane conductance regulator (CFTR), leading to the rapid degradation of CFTR molecules that have not matured beyond the endoplasmic reticulum (ER). The mechanism by which integral membrane proteins including CFTR are recognized and targeted for ER degradation and the proteolytic machinery involved in this process are not well understood. We show here that the degradation of both wild-type and mutant CFTR is inhibited by two potent proteasome inhibitors that induce the accumulation of polyubiquitinated forms of immature CFTR. CFTR degradation was also inhibited by coexpression of a dominant negative ubiquitin mutant and in cells bearing a temperature-sensitive mutation in the ubiquitin-activating enzyme, confirming that ubiquitination is required for rapid CFTR degradation.
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Cites
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Cited by
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Aggresomes: A Cellular Response to Misfolded Proteins
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Self-citationLung Infections Associated with Cystic Fibrosis
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Metadata
- Authors
- Ward, C. L., Omura, S., & Kopito, R. R.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-10
- Volume
- 83
- Issue
- 1
- Pages
- 121-127
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2015357935
- Cited by
- 1,304
- References
- 31
- FWCI
- 77.21
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Ward, C. L., Omura, S., & Kopito, R. R. (1995). Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. https://doi.org/10.1016/0092-8674(95)90240-6
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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.
