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

Kristijan Ramadan, Roland Bruderer, Fabio M. Spiga, Oliver Popp, Tina Baur, Monica Gotta and Hemmo H. Meyer ()
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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
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
Hemmo H. Meyer: Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland

Nature, 2007, vol. 450, issue 7173, 1258-1262

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.

Date: 2007
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DOI: 10.1038/nature06388

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