Cdc48/p97 mediates UV-dependent turnover of RNA Pol II
Open accessAbstract
Cdc48/p97 is an essential ATPase whose role in targeting substrates to the ubiquitin-proteasome system (UPS) remains unclear. Existing models posit that Cdc48 acts upstream of UPS receptors. To address this hypothesis, we examined the association of ubiquitin (Ub) conjugates with 26S proteasomes. Unexpectedly, proteasomes isolated from cdc48 mutants contain high levels of Ub conjugates, and mass spectrometry identified numerous nonproteasomal proteins, including Rpb1, the largest subunit of RNA Pol II. UV-induced turnover of Rpb1 depends upon Cdc48-Ufd1-Npl4, Ubx4, and the uncharacterized adaptor Ubx5. Ubiquitinated Rpb1, proteasomes, and Cdc48 accumulate on chromatin in UV-treated wild-type cells, and the former two accumulate to higher levels in mutant cells, suggesting that degradation of Rpb1 is facilitated by Cdc48 at sites of stalled transcription. These data reveal an intimate coupling of function between proteasomes and Cdc48 that we suggest is necessary to sustain processive degradation of unstable subunits of some macromolecular protein complexes.
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AAA+ ATPase p97 unfoldase activity is necessary for extracting a subset of proteins marked for degradation from multi-protein complexes, chromatin, or membrane bound complexes.
“AAA+ ATPase p97 unfoldase activity has been demonstrated to be necessary for extracting a subset of proteins marked for degradation from multi-protein complexes, chromatin, or membrane bound complexes (Ramadan et al., 2007; Shcherbik and Haines, 2007; Verma et al., 2011).”
From Mapping the Degradable Kinome Provides a Resource for Expedited Degrader Development (2020) · cites this paper as Verma et al., 2011
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References 76 · Cited by 196
- Authors
- Verma, R., Oania, R., Fang, R., Smith, G. T., & Deshaies, R. J.
- Affiliations
- California Institute of Technology (US)
- Corresponding author
- Verma, Rati
- Deshaies, Raymond J.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2011-01
- Volume
- 41
- Issue
- 1
- Pages
- 82-92
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC3063307
- OpenAlex
- W2047350942
- Cited by
- 196
- References
- 76
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 12 · 2023: 9 · 2022: 11 · 2021: 11 · 2020: 12 · 2019: 13 · 2018: 7 · 2017: 14 · 2016: 17 · 2015: 10 · 2014: 17 · 2013: 24 · 2012: 17
- FWCI
- 9.62
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Keywords
- Cdc48/p97, RNA polymerase II, RPB1, ubiquitin-proteasome system, proteasome, transcriptional stalling, ATPase
- MeSH terms
- Valosin Containing Protein, Adenosine Triphosphatases, Carrier Proteins, Models, Genetic, RNA Polymerase II, Saccharomyces cerevisiae, Ultraviolet Rays, Mutagenesis, Gene Deletion, Cell Cycle Proteins, Ubiquitin, Saccharomyces cerevisiae Proteins, Cullin Proteins, Proteasome Endopeptidase Complex, Intracellular Signaling Peptides and Proteins, Ubiquitination, Protein Unfolding
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