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

Author

Listed:
  • Kristijan Ramadan

    (Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland)

  • Roland Bruderer

    (Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland)

  • Fabio M. Spiga

    (Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland
    University of Geneva School of Medicine, Rue Michel-Servet 1, 1211 Geneva 4, Switzerland)

  • Oliver Popp

    (Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland)

  • Tina Baur

    (Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland)

  • Monica Gotta

    (Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland
    University of Geneva School of Medicine, Rue Michel-Servet 1, 1211 Geneva 4, Switzerland)

  • Hemmo H. Meyer

    (Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland)

Abstract

At the onset of mitosis, the nuclear envelope is diassembled, and is reformed at the end of the process. A mechanistic explanation for the reformation of the nuclear envelope is provided, finding that the chaperone p97 (an AAA ATPase) binds to an ubiquitylated form of Aurora B, an inhibitor of nuclear envelope formation, on chromatin. This results in extraction of Aurora B from chromatin, allowing chromosome decondensation and nuclear envelope formation.

Suggested Citation

  • Kristijan Ramadan & Roland Bruderer & Fabio M. Spiga & Oliver Popp & Tina Baur & Monica Gotta & Hemmo H. Meyer, 2007. "Cdc48/p97 promotes reformation of the nucleus by extracting the kinase Aurora B from chromatin," Nature, Nature, vol. 450(7173), pages 1258-1262, December.
  • Handle: RePEc:nat:nature:v:450:y:2007:i:7173:d:10.1038_nature06388
    DOI: 10.1038/nature06388
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