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.
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28 May 2002
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May 28 2002
The Rho-associated protein kinase p160ROCK is required for centrosome positioning
Véronique Chevrier,
Véronique Chevrier
1Institut 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
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Matthieu Piel,
Matthieu Piel
2Institut Curie, Section Recherche, UMR 144 du Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France
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Nora Collomb,
Nora Collomb
1Institut 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
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Yasmina Saoudi,
Yasmina Saoudi
1Institut 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
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Ronald Frank,
Ronald Frank
3AG Molecular Recognition, Gesellschaft für Biotechnologische Forschung, D-38124 Braunschweig, Germany
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Michel Paintrand,
Michel Paintrand
1Institut 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
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Shuh Narumiya,
Shuh Narumiya
4Department of Pharmacology, Kyoto University Faculty of Medicine, Sako-ku, Kyoto 606, Japan
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Michel Bornens,
Michel Bornens
2Institut Curie, Section Recherche, UMR 144 du Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France
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Didier Job
Didier Job
1Institut 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
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Véronique Chevrier
1Institut 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
Matthieu Piel
2Institut Curie, Section Recherche, UMR 144 du Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France
Nora Collomb
1Institut 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
Yasmina Saoudi
1Institut 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
Ronald Frank
3AG Molecular Recognition, Gesellschaft für Biotechnologische Forschung, D-38124 Braunschweig, Germany
Michel Paintrand
1Institut 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
Shuh Narumiya
4Department of Pharmacology, Kyoto University Faculty of Medicine, Sako-ku, Kyoto 606, Japan
Michel Bornens
2Institut Curie, Section Recherche, UMR 144 du Centre National de la Recherche Scientifique, 75248 Paris Cedex 05, France
Didier Job
1Institut 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
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: [email protected]
V. Chevrier and M. Piel contributed equally to this work.
*
Abbreviations used in this paper: CD, cytochalasin D; DC, daughter centriole; GFP, green fluorescent protein; MC, mother centriole; nt, nucleotide; ROCK, Rho-associated coiled-coil–containing protein kinase; PCM, pericentriolar material.
Received:
March 07 2002
Revision Received:
April 15 2002
Accepted:
April 16 2002
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2002
J Cell Biol (2002) 157 (5): 807–817.
Article history
Received:
March 07 2002
Revision Received:
April 15 2002
Accepted:
April 16 2002
Citation
Véronique Chevrier, Matthieu Piel, Nora Collomb, Yasmina Saoudi, Ronald Frank, Michel Paintrand, Shuh Narumiya, Michel Bornens, Didier Job; The Rho-associated protein kinase p160ROCK is required for centrosome positioning . J Cell Biol 28 May 2002; 157 (5): 807–817. doi: https://doi.org/10.1083/jcb.200203034
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