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

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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

DOI 10.1038/nature06388

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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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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.
ORCID: Ramadan, Kristijan
Bruderer, Roland
Spiga, Fabio M.
Popp, Oliver
Gotta, Monica
Meyer, Hemmo H.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2007-12
Volume: 450
Issue: 7173
Pages: 1258-1262
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature06388
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: green
archive-ouverte.unige.ch
Licence: cc-by
www.springer.com/tdm (tdm)
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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Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin

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