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J. Biol. Chem., Vol. 279, Issue 38, 40091-40099, September 17, 2004

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A Novel Dynamin-associating Molecule, Formin-binding Protein 17, Induces Tubular Membrane Invaginations and Participates in Endocytosis^*

Yuji Kamioka, Shigetomo Fukuhara, Hirofumi Sawa, Kazuo Nagashima, Michitaka Masuda, Michiyuki Matsuda¶, and Naoki Mochizuki||

From the Department of Structural Analysis, National Cardiovascular Center Research Institute, 5-7-1 Fujishirodai, Suita, Osaka 565-8565, Japan, the Laboratory of Molecular and Cellular Pathology, Hokkaido University School of Medicine, Sapporo 060-8638, Japan, and the ^¶Department of Tumor Virology, Research Institute for Microbial Disease, Osaka University, Osaka 565-0871, Japan

Dynamin associates with a variety of SH3 domain-containing molecules via a C-terminal proline-rich motif and takes part, with them, in endocytic processes. Here, we have investigated a new dynamin-associating molecule, formin-binding protein 17 (FBP17), involved in deforming the plasma membrane and in endocytosis. FBP17 formed tubular invaginations originating from the plasma membrane. Its N-terminal Fer/CIP4 homology domain, a coiled-coil domain, and a proline-rich motif were required for tubular invagination and self-assembly, by which tubular invagination might be induced. Using anti-FBP17 antibody, we detected positive immunoreactions in the testis that were restricted to the germ cells. We also detected FBP17 in the brain by immunoblotting and in situ hybridization. When COS cells expressing enhanced green fluorescent protein-tagged FBP17 were incubated with fluorescently labeled transferrin, epidermal growth factor, and cholera toxin, these molecules co-localized with FBP17-induced tubular invaginations, suggesting that FBP17 is involved in dynamin-mediated endocytosis in both a clathrin-dependent and -independent manner. These observations therefore indicate that FBP17 interacts with dynamin and regulates endocytosis by forming vesicotubular structures.

Received for publication, May 3, 2004 , and in revised form, June 17, 2004.

^* This work was supported in part by grants from the Ministry of Health, Labor, and Welfare of Japan; the Promotion of Fundamental Studies in Health Science of the Organization for Pharmaceutical Safety and Research of Japan; the Ministry of Education, Science, Sports, and Culture of Japan; the Cell Science Research Foundation; the Uehara Memorial Foundation; and the Takeda Medical Research Foundation. 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.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Figs. 1 and 2 and Videos 1 and 2.

^|| To whom correspondence should be addressed. Tel.: 81-6-6833-5012 (ext. 2508); Fax: 81-6-6835-5461; E-mail: nmochizu{at}ri.ncvc.go.jp.

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