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J Biol Chem, Vol. 273, Issue 30, 18697-18700, July 24, 1998

COMMUNICATION
Frabin, a Novel FGD1-related Actin Filament-binding Protein Capable of Changing Cell Shape and Activating c-Jun N-terminal Kinase

Hiroshi Obaishi, Hiroyuki Nakanishi, Kenji Mandai, Keiko Satoh, Ayako Satoh, Kenichi Takahashi, Masako Miyahara, Hideo Nishioka, Kenji Takaishi^§, and Yoshimi Takai^§

From the  Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, c/o JCR Pharmaceuticals Co., Ltd., 2-2-10 Murotani, Nishi-ku, Kobe 651-2241, Japan and the ^§ Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita 565-0871, Japan

We purified from rat brain a novel F-actin-binding protein with a M_r of about 105,000 (p105), which was estimated by SDS-polyacrylamide gel electrophoresis. We cloned its cDNA from a rat brain cDNA library and characterized it. p105 was a protein of 766 amino acids and showed a calculated M_r of 86,449. p105 consisted of one F-actin-binding domain at the N-terminal region, one Dbl homology domain and one pleckstrin homology domain at the middle region, and one cysteine-rich domain at the C-terminal region. This domain organization of p105 was similar to that of FGD1, which has been determined to be the genetic locus responsible for faciogenital dysplasia or Aarskog-Scott syndrome. We therefore named p105 frabin (FGD1-related F-actin-binding protein). Frabin bound along the sides of F-actin and showed F-actin-cross-linking activity. Overexpression of frabin in Swiss 3T3 cells and COS7 cells induced cell shape change and c-Jun N-terminal kinase activation, respectively, as described for FGD1. Because FGD1 has been shown to serve as a GDP/GTP exchange protein for Cdc42 small G protein, it is likely that frabin is a direct linker between Cdc42 and the actin cytoskeleton.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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