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Vol. 14, Issue 10, 4260-4271, October 2003
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¶
Institut Curie, Section Recherche, Unité Mixte Recherche 144-Centre National de la Recherche Scientifique, 75248 Paris, France;
Institute of Molecular Biology and Pathology-Consiglio Nazionale delle Ricerche c/o Università "La Sapienza," Rome, Italy;
Department of Botany, University of Cologne, Cologne, Germany; and
|| School of Biological Sciences, University of East Anglia, Norwich, Norfolk NR4 7TJ, United Kingdom
Submitted November 28, 2002;
Revised June 6, 2003;
Accepted June 6, 2003
Monitoring Editor: Ted Salmon
The small Ran GTPase, a key regulator of nucleocytoplasmic transport, is also involved in microtubule assembly and nuclear membrane formation. Herein, we show by immunofluorescence, immunoelectron microscopy, and biochemical analysis that a fraction of Ran is tightly associated with the centrosome throughout the cell cycle. Ran interaction with the centrosome is mediated by the centrosomal matrix A kinase anchoring protein (AKAP450). Accordingly, when AKAP450 is delocalized from the centrosome, Ran is also delocalized, and as a consequence, microtubule regrowth or anchoring is altered, despite the persisting association of 
-tubulin with the centrosome. Moreover, Ran is recruited to Xenopus sperm centrosome during its activation for microtubule nucleation. We also demonstrate that centrosomal proteins such as centrin and pericentrin, but not -tubulin, AKAP450, or ninein, undertake a nucleocytoplasmic exchange as they concentrate in the nucleus upon export inhibition by leptomycin B. Together, these results suggest a challenging possibility, namely, that centrosome activity could depend upon nucleocytoplasmic exchange of centrosomal proteins and local Ran-dependent concentration at the centrosome.
* These authors contributed equally to this work.
¶ Corresponding author. E-mail address: atassin{at}curie.fr.
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