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

Areas: Cell Cycle
The nucleus reformation during mitosis is stimulated by hexameric ATPase p97 that inactivates the chromatin-associated kinase Aurora B. Kristijan Ramadan and Roland Bruderer from the ETH in Zurich, Switzerland, observed Aurora B to inhibit nucleus reformation by preventing decondensation of the chromosomes and arrangement of a nuclear double-membrane around the chromatin, two processes required for nucleus reformation.
On exit of mitosis, p97 binds to Aurora B and removes it from the chromatin. Aurora B thus becomes inactivated and chromatin decondensation and nuclear membrane formation can take place. Protein extraction is apparently a common mechanism of Cdc48/p97 activity in nucleus reformation.

Related antibodies on antibodies-online.com:

ATPase p97

Aurora B

Ubiquitin

Antibodies for the research area cell cycle: »Show antibodies

29.01.2008  |  Anna Lena Marwedel      RSS Feed  Research News


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