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Originally published as MBC in Press, 10.1091/mbc.E06-12-1140 on December 19, 2007

Vol. 19, Issue 3, 1220-1229, March 2008

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Inhibition of Proteasome Activity Impairs Centrosome-dependent Microtubule Nucleation and Organization

Christine Didier*, Andreas Merdes, Jean-Edouard Gairin, and Nabila Jabrane-Ferrat{dagger}

Institut de Sciences et Technologies du Médicament de Toulouse, Unité Mixte de Recherche 2587 Centre National de la Recherche Scientifique-Pierre Fabre, 31400 Toulouse, France

Submitted December 21, 2006; Revised November 26, 2007; Accepted December 12, 2007
Monitoring Editor: Yixian Zheng

Centrosomes are dynamic organelles that consist of a pair of cylindrical centrioles, surrounded by pericentriolar material. The pericentriolar material contains factors that are involved in microtubule nucleation and organization, and its recruitment varies during the cell cycle. We report here that proteasome inhibition in HeLa cells induces the accumulation of several proteins at the pericentriolar material, including gamma-tubulin, GCP4, NEDD1, ninein, pericentrin, dynactin, and PCM-1. The effect of proteasome inhibition on centrosome proteins does not require intact microtubules and is reversed after removal of proteasome inhibitors. This accrual of centrosome proteins is paralleled by accumulation of ubiquitin in the same area and increased polyubiquitylation of nonsoluble gamma-tubulin. Cells that have accumulated centrosome proteins in response to proteasome inhibition are impaired in microtubule aster formation. Our data point toward a role of the proteasome in the turnover of centrosome proteins, to maintain proper centrosome function.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-12-1140) on December 19, 2007.

* Present address: LBCMCP, UMR5088, CNRS 118 Route de Narbonne Toulouse, 31400 France.

{dagger} Present address: Institut National de la Santé et de la Recherche Medicale U563, CPTP, CHU Purpan, BP 3028, 31024 Toulouse Cedex 3, France.

Address correspondence to: Nabila Jabrane-Ferrat (nabila.jabrane-ferrat{at}toulouse.inserm.fr)






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