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¹ Institut National de la Santé et de la Recherche Medicale U366, Département de Biologie Moléculaire et Structurale/Cytosqulette, Commissariat à l'Energie Atomique, de Grenoble, 38054 Grenoble Cedex 9, France
² Institut Curie, Section Recherche, UMR 144 du Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France
³ AG Molecular Recognition, Gesellschaft für Biotechnologische Forschung, D-38124 Braunschweig, Germany
⁴ Department of Pharmacology, Kyoto University Faculty of Medicine, Sako-ku, Kyoto 606, Japan

Address correspondence to Didier Job, INSERM U366, DBMS/CS, CEA de Grenoble, 17 Rue des Martyrs, 38054 Grenoble Cedex 9, France. Tel.: 33-04-38-78-51-00. Fax: 33-04-38-78-50-57. E-mail: djob{at}cea.fr

The p160–Rho-associated coiled-coil–containing protein kinase (ROCK) is identified as a new centrosomal component. Using immunofluorescence with a variety of p160ROCK antibodies, immuno EM, and depletion with RNA interference, p160ROCK is principally bound to the mother centriole (MC) and an intercentriolar linker. Inhibition of p160ROCK provoked centrosome splitting in G1 with the MC, which is normally positioned at the cell center and shows little motion during G1, displaying wide excursions around the cell periphery, similar to its migration toward the midbody during cytokinesis. p160ROCK inhibition late after anaphase in mitosis triggered MC migration to the midbody followed by completion of cell division. Thus, p160ROCK is required for centrosome positioning and centrosome-dependent exit from mitosis.

Key Words: centrosome; structure; motion; p160ROCK; cytokinesis

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