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Originally published In Press as doi:10.1074/jbc.C000806200 on January 22, 2001

J. Biol. Chem., Vol. 276, Issue 14, 10581-10584, April 6, 2001
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ACCELERATED PUBLICATION
Leucine Zipper-mediated Homodimerization of the p21-activated Kinase-interacting Factor, beta Pix
IMPLICATION FOR A ROLE IN CYTOSKELETAL REORGANIZATION*

Seyun Kim, Seung-Hye Lee, and Dongeun ParkDagger

From the School of Biological Sciences, Seoul National University, Seoul 151-742, Republic of Korea

Pix, a p21-activated kinase-interacting exchange factor, is known to be involved in the regulation of Cdc42/Rac GTPases. The 85-kDa beta Pix-a protein contains an Src homology 3 domain, the tandem Dbl homology and Pleckstrin homology domains, a proline-rich region, and a GIT1-binding domain. In addition to those domains, beta Pix-a also contains a putative leucine zipper domain at the C-terminal end. In this study, we demonstrate that the previously identified putative leucine zipper domain mediates the formation of beta Pix-a homodimers. Using in vitro and in vivo methodologies, we show that deletion of the leucine zipper domain is sufficient to abolish beta Pix-a homodimerization. In NIH3T3 fibroblast cells, expression of wild type beta Pix-a induces the formation of membrane ruffles. However, cells expressing the leucine zipper domain deletion mutant could not form membrane ruffle structures. Moreover, platelet-derived growth factor-mediated cytoskeletal changes were completely blocked by the leucine zipper domain deletion mutant. The results suggest that the leucine zipper domain enables beta Pix-a to homodimerize, and homodimerization is essential for beta Pix-a signaling functions leading to the cytoskeletal reorganization.

* This work was supported in part by Korea Science Foundation (KOSEF) Grant 1998G0202 through Center for Cell Signaling Research and by KOSEF Grant 97-0401-07-01-5. S. K. and S.-H. L. were supported by Fellowship BK21 from the Korean Ministry of Education.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: School of Biological Sciences, Seoul National University, Kwanak-gu, Shilim-dong, Seoul 151-742, Republic of Korea. Tel.: 82-2-880-5753; Fax: 82-2-872-1993; E-mail: depark@snu.ac.kr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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