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Originally published In Press as doi:10.1074/jbc.M304522200 on May 11, 2003

J. Biol. Chem., Vol. 278, Issue 30, 27844-27852, July 25, 2003
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M Phase Phosphoprotein 1 Is a Human Plus-end-directed Kinesin-related Protein Required for Cytokinesis*

Aouatef Abaza {ddagger} § ¶, Jean-Marc Soleilhac {ddagger} ¶, Joanne Westendorf {ddagger} ||, Matthieu Piel **, Isabelle Crevel {ddagger}{ddagger}, Aurélien Roux §§ and Fabienne Pirollet {ddagger} ¶¶

From the {ddagger}INSERM U366, Département Réponse et Dynamique Cellulaires, Laboratoire du Cytosquelette, Commissariat à l'Energie Atomique-Grenoble, 17 rue des Martyrs, 38 054 Grenoble Cedex 9, France, **Institut Curie, Section Recherche, UMR 144 du CNRS, 75 248 Paris Cedex 05, France, {ddagger}{ddagger}Marie Curie Research Institute, Oxted RH8 OTL, United Kingdom, and §§Institut Curie, Section Recherche, UMR 168 du CNRS, 75 248 Paris Cedex 05, France

The human M phase phosphoprotein 1 (MPP1), previously identified through a screening of a subset of proteins specifically phosphorylated at the G2/M transition (Matsumoto-Taniura, N., Pirollet, F., Monroe, R., Gerace, L., and Westendorf, J. M. (1996) Mol. Biol. Cell 7, 1455–1469), is characterized as a plus-end-directed kinesin-related protein. Recombinant MPP1 exhibits in vitro microtubule-binding and microtubule-bundling properties as well as microtubule-stimulated ATPase activity. In gliding experiments using polarity-marked microtubules, MPP1 is a slow molecular motor that moves toward the microtubule plus-end at a 0.07 µm/s speed. In cycling cells, MPP1 localizes mainly to the nuclei in interphase. During mitosis, MPP1 is diffuse throughout the cytoplasm in metaphase and subsequently localizes to the midzone to further concentrate on the midbody. MPP1 suppression by RNA interference induces failure of cell division late in cytokinesis. We conclude that MPP1 is a new mitotic molecular motor required for completion of cytokinesis.


Received for publication, April 30, 2003

* This work was supported by Ligue Nationale contre le Cancer Grant 10V04 and Association pour la Recherche contre le Cancer Grant 9857 (to F. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Recipient of French Research Ministry and Fondation pour la Recherche Médicale fellowships.

These two authors contributed equally to this work.

|| Supported by fellowships from Association pour la Recherche contre le Cancer and Fondation pour la Recherche Médicale.

¶¶ To whom correspondence should be addressed. Tel. 33-4-38-78-54-82; Fax: 33-4-38-78-50-57; E-mail: fpirollet{at}cea.fr.


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