The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Mobilization of Processed, Membrane-Tethered SPT23 Transcription Factor by CDC48UFD1/NPL4, a Ubiquitin-Selective Chaperone
Open accessAbstract
The OLE pathway of yeast regulates the level of the ER-bound enzyme Delta9-fatty acid desaturase OLE1, thereby controlling membrane fluidity. A central component of this regulon is the transcription factor SPT23, a homolog of mammalian NF-kappaB. SPT23 is synthesized as an inactive, ER membrane-anchored precursor that is activated by regulated ubiquitin/proteasome-dependent processing (RUP). We now show that SPT23 dimerizes prior to processing and that the processed molecule, p90, retains its ubiquitin modification and initially remains tethered to its unprocessed, membrane-bound SPT23 partner. Subsequently, p90 is liberated from its partner for nuclear targeting by the activity of the chaperone-like CDC48(UFD1/NPL4) complex. Remarkably, this enzyme binds preferentially ubiquitinated substrates, suggesting that CDC48(UFD1/NPL4) is qualified to selectively remove ubiquitin conjugates from protein complexes.
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Cited by
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ER-associated degradation in protein quality control and cellular regulation
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Metadata
- Authors
- Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H., & Jentsch, S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2001-11
- Volume
- 107
- Issue
- 5
- Pages
- 667-677
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2122551230
- Cited by
- 438
- References
- 34
- FWCI
- 9.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H., & Jentsch, S. (2001). Mobilization of Processed, Membrane-Tethered SPT23 Transcription Factor by CDC48UFD1/NPL4, a Ubiquitin-Selective Chaperone. Cell. https://doi.org/10.1016/s0092-8674(01)00595-5
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