View the Current Issue

Article

  • The EMBO Journal (2001) 20, 2878 - 2884
  • doi:10.1093/emboj/20.11.2878

Requirement of Hsp90 for centrosomal function reflects its regulation of Polo kinase stability

Guillermo de Cárcer1, Maria do Carmo Avides2, María José Lallena3, David M. Glover2 and Cayetano González1

  1. Cell Biology and Biophysics, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany
  2. Cancer Research Campaign Cell Cycle Genetics Group, University of Cambridge, Department of Genetics, Downing Street, Cambridge CB2 3EH, UK
  3. Gene Expression Programmes, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany

Correspondence to:

Cayetano González, E-mail: gonzalez@embl-heidelberg.de

Received 7 November 2000; Accepted 29 March 2001; Revised 13 March 2001

We have previously shown that the molecular chaperone heat shock protein 90 (Hsp90) is required to ensure proper centrosome function in Drosophila and vertebrate cells. This observation led to the hypothesis that this chaperone could be required for the stability of one or more centrosomal proteins. We have found that one of these is Polo, a protein kinase known to regulate several aspects of cell division including centrosome maturation and function. Inhibition of Hsp90 results in the inactivation of Polo kinase activity. It also leads to a loss in the ability of cytoplasmic extracts to complement the failure of salt-stripped preparations of centrosomes to nucleate microtubules. This effect can be rescued upon addition of active recombinant Polo. We also show that Polo and Hsp90 are part of a complex and conclude that stabilization of Polo is one of the mechanisms by which Hsp90 contributes to the maintenance of functional centrosomes.

  • Keywords:

    • centrosome,
    • Drosophila,
    • Hsp90,
    • Polo