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J. Biol. Chem., Vol. 280, Issue 45, 37901-37907, November 11, 2005

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Local Change in Phospholipid Composition at the Cleavage Furrow Is Essential for Completion of Cytokinesis^*

Kazuo Emoto1, Hironori Inadome, Yasunori Kanaho, Shuh Narumiya¶, and Masato Umeda2

From the Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan, The Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, Tokyo 113-8613, Japan, and ^¶Department of Pharmacology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8315, Japan

Cell division ends up with the membrane separation of two daughter cells, presumably by a membrane fusion that requires dynamic changes of the distribution and the composition of membrane lipids. We have previously shown that a membrane lipid phosphatidylethanolamine (PE) is exposed on the cell surface of the cleavage furrow during late cytokinesis and that this PE movement is involved in regulation of the contractile ring disassembly. Here we show that immobilization of cell surface PE by a PE-binding peptide blocks the RhoA inactivation in the late stage of cytokinesis. Phosphatidylinositol 4-phosphate 5-kinase (PIP5K), but not other RhoA effectors, is co-localized with RhoA in the peptide-treated cells. Indeed, PIP5K and its product phosphatidylinositol 4,5-bisphosphate (PI(4,5)P₂) are localized to the cleavage furrow of normally dividing cells. Both overexpression of a kinase-deficient PIP5K mutant and microinjection of anti-PI(4,5)P₂ antibodies compromise cytokinesis by preventing local accumulation of PI(4,5)P₂ in the cleavage furrow. These findings demonstrate that the localized production of PI(4,5)P₂ is required for the proper completion of cytokinesis and that the possible formation of a unique lipid domain in the cleavage furrow membrane may play a crucial role in coordinating the contractile rearrangement with the membrane remodeling during late cytokinesis.

Received for publication, April 19, 2005 , and in revised form, August 23, 2005.

^* 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.

¹ Present address: Howard Hughes Medical Institute, Department of Physiology and Biochemistry, University of California San Francisco, 1550 4th St., San Francisco, CA 94143.

² To whom correspondence should be addressed: Div. of Supramolecular Biology, Institute for Chemical Research, Uji, Kyoto 611-0011, Japan. Tel.: 81-774-38-3250; Fax: 81-774-38-3256; E-mail: umeda{at}scl.kyoto-u.ac.jp.

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