The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin
Open accessAbstract
During division of metazoan cells, the nucleus disassembles to allow chromosome segregation, and then reforms in each daughter cell. Reformation of the nucleus involves chromatin decondensation and assembly of the double-membrane nuclear envelope around the chromatin; however, regulation of the process is still poorly understood. In vitro, nucleus formation requires p97 (ref. 3), a hexameric ATPase implicated in membrane fusion and ubiquitin-dependent processes. However, the role and relevance of p97 in nucleus formation have remained controversial. Here we show that p97 stimulates nucleus reformation by inactivating the chromatin-associated kinase Aurora B. During mitosis, Aurora B inhibits nucleus reformation by preventing chromosome decondensation and formation of the nuclear envelope membrane. During exit from mitosis, p97 binds to Aurora B after its ubiquitylation and extracts it from chromatin. This leads to inactivation of Aurora B on chromatin, thus allowing chromatin decondensation and nuclear envelope formation. These data reveal an essential pathway that regulates reformation of the nucleus after mitosis and defines ubiquitin-dependent protein extraction as a common mechanism of Cdc48/p97 activity also during nucleus formation.
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“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 Ramadan et al., 2007
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Cites
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Self-citationERAD: the long road to destruction
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Chapter 30 Cell Cycle Extracts
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Histone H3 serine 10 phosphorylation by Aurora B causes HP1 dissociation from heterochromatin
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Function of the p97–Ufd1–Npl4 complex in retrotranslocation from the ER to the cytosol
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Self-citationp47 is a cofactor for p97-mediated membrane fusion
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Self-citationCatastrophic nuclear envelope collapse in cancer cell micronuclei
Hatch, E. M., Fischer, A. H., Deerinck, T. J., & Hetzer, M. W. (2013) · Cell · doi:10.1016/j.cell.2013.06.007 · Cited by 741
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Survivin Reads Phosphorylated Histone H3 Threonine 3 to Activate the Mitotic Kinase Aurora B
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Metadata
- Authors
- Ramadan, K., Bruderer, R., Spiga, F. M., Popp, O., Baur, T., Gotta, M., & Meyer, H. H.
- Affiliations
- ETH Zurich (CH)
- University of Geneva (CH)
- Corresponding author
- Meyer, Hemmo H.
- Venue
- Nature
- Published
- 2007-12
- Volume
- 450
- Issue
- 7173
- Pages
- 1258-1262
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1981835453
- Cited by
- 261
- References
- 33
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 7 · 2023: 10 · 2022: 13 · 2021: 7 · 2020: 16 · 2019: 8 · 2018: 8 · 2017: 16 · 2016: 15 · 2015: 13 · 2014: 20 · 2013: 17 · 2012: 29
- FWCI
- 6.09
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- Cdc48/p97, Aurora B kinase, nuclear envelope reformation, mitosis, chromatin decondensation, ubiquitination, AAA+ ATPase, nuclear envelope assembly, chromosome segregation
- MeSH terms
- Valosin Containing Protein, Adenosine Triphosphatases, Animals, Cell Nucleus, Chromatin, Female, Male, Nuclear Envelope, Xenopus laevis, Caenorhabditis elegans, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Ubiquitin, RNA Interference, Ubiquitination, Aurora Kinases
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