Cited by 261Nuclear Structure and FunctionMicrotubule and mitosis dynamicsUbiquitin and proteasome pathways

Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin

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Ramadan, Kristijan, Bruderer, Roland, Spiga, Fabio M., Popp, Oliver, Baur, Tina, Gotta, Monica, Meyer, Hemmo H.·2007·Nature

Abstract

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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Crossref · 10.1038/nature06388

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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 Ramadan et al., 2007

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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
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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