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A more recent version of this article appeared on June 1, 2003
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Submitted on September 25, 2002
Revised on December 27, 2002
Accepted on January 23, 2003
1 UMR 144-CNRS-Institut Curie, 26 rue d'Ulm, F-75248, Paris cedex 05, France
2 Department of Medical Biochemistry, Institute of Basic Medical Sciences, University of Oslo, N-0317 Oslo, Norway
3 Department of Biochemistry, Max-Planck-Institute for Developmental Biology D-72076 Tübingen, Germany
4 UMR 147-CNRS-Institut Curie, 26 rue d'Ulm, F-75248, Paris cedex 05, France
* Corresponding author. E-mail address: Michel.Bornens{at}curie.fr.
Centrosomes provide docking sites for regulatory molecules involved in the control of the cell division cycle. The centrosomal matrix contains several proteins, which anchor kinases and phosphatases. The large A-Kinase Anchoring Protein AKAP450 (CG-NAP/AKAP350) is acting as a scaffolding protein for other components of the cell signaling machinery. We selectively perturbed the centrosome by modifying the cellular localization of AKAP450. We report that the expression in HeLa cells of the C-terminus of AKAP450, which contains the centrosome targeting domain of AKAP450 but not its coiled-coil domains or binding sites for signaling molecules, leads to the displacement of the endogenous centrosomal AKAP450 without removing centriolar or peri-centrosomal components such as centrin, gamma-tubulin or pericentrin. The centrosomal PKA type II alpha anchored to AKAP450 was delocalized. We further show that this expression impairs cytokinesis and increases ploidy in HeLa cells. By contrast it arrests diploid RPE1 fibroblasts in G1 thus further establishing a role of the centrosome in the regula tion of the cell division cycle. Moreover, centriole duplication is interrupted. Our data show that the association between centrioles and the centrosomal matrix protein AKAP450 is critical for the integrity of the centrosome and for its reproduction.
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