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A role for Cdc48/p97 and Aurora B in controlling chromatin condensation during exit from mitosis

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During cell division, chromosomes condense so that the replicated chromatids can be segregated by the mitotic spindle. While condensation is governed by cyclin-dependent kinase 1 (Cdk1) during mitotic entry and early mitosis, it is still poorly understood how condensation is maintained during anaphase after Cdk1 inactivation, and how decondensation is triggered in telophase. Here, we review recent reports that point to a novel role of Aurora B kinase in maintaining condensation and preventing premature nuclear envelope formation during exit from mitosis. Timely decondensation and nuclear envelope formation at the end of mitosis may then be triggered by two mechanisms. One is removing Aurora B phosphorylation marks from chromatin by specific phosphatases. The other is removing and inactivating Aurora B kinase itself by the ubiquitin system. We have recently provided evidence that the AAA ATPase Cdc48/p97 plays a central role in the inactivation of Aurora B, as it extracts ubiquitinated Aurora B from chromosomes and thus reduces chromatinassociated Aurora B activity.

Lors de la division cellulaire, les chromosomes se condensent afin que les chromatides répliquées puissent être séparées par le fuseau mitotique. Alors que la condensation est gouvernée par la kinase dépendante de la cycline 1 (Cdk1) lors de l’entrée en mitose et la mitose précoce, on comprend encore mal comment la condensation est maintenue lors de l’anaphase, après l’inactivation de Cdk1, et comment la décondensation s’amorce lors de la télophase. Nous passons ici en revue les données récentes qui proposent un nouveau rôle de la kinase Aurora B dans le maintien de la condensation et dans la prévention de la formation prématurée de l’enveloppe nucléaire lors de la sortie de mitose. La décondensation en temps opportun et la formation de l’enveloppe nucléaire à la fin de la mitose peuvent ainsi être provoquées par deux mécanismes. Le premier consiste à enlever les marques de phosphorylation catalysées par Aurora B sur la chromatine à l’aide de phosphatases spécifiques. L’autre consiste à enlever et inactiver la kinase Aurora B elle-même par le système de l’ubiquitine. Nous avons récemment prouvé que l’ATPase à domaine AAA Cdc48/p97 joue un rôle clé dans l’inactivation d’Aurora B car elle extrait l’Aurora B ubiquitinée des chromosomes et réduit ainsi l’activité d’Aurora B associée à la chromatine.

Document Type: Research Article

Publication date: 2010-02-01

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  • Published since 1929, this bimonthly journal explores every aspect of general biochemistry and includes up-to-date coverage of experimental research into cellular and molecular biology, as well as review articles on topics of current interest and notes contributed by recognized international experts. Special issues each year are dedicated to expanding new areas of research in biochemistry and cell biology.
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