Open Access

A method for analyzing the ubiquitination and degradation of aurora-A

  • Andrea Klotzbucher1,
  • Gaetan Pascreau2,
  • Claude Prigent2 and
  • Yannick Arlot-Bonnemains2Email author
Biological Procedures Online4:41062

https://doi.org/10.1251/bpo35

Received: 22 August 2002

Accepted: 27 September 2002

Abstract

The cell cycle machinery consists of regulatory proteins that control the progression through the cell cycle ensuring that DNA replication alternates with DNA segregation in mitosis to maintain cell integrity. Some of these key regulators have to be degraded at each cell cycle to prevent cellular dysfunction. Mitotic exit requires the inactivation of cyclin dependent kinase1 (cdk1) and it is the degradation of the cyclin subunit that inactivates the kinase. Cyclin degradation has been well characterized and it was shown that it is ubiquitin proteasome pathway that leads to the elimination of cyclins. By now, many other regulatory proteins were shown to be degraded by the same pathway, among them members of the aurora kinase family, degraded many other regulatory proteins. Aurora kinases are involved in mitotic spindle formation as well as in cytokinesis. The abundance and activity of the kinase is precisely regulated during the cell cycle. To understand how proteolysis regulates transitions through the cell cycle we describe two assays for ubiquitination and degradation of xenopus aurora kinase A using extracts from xenopus eggs or somatic cell lines.

Indexing terms

Xenopus ubiquitin

Notes

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