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Papers In Press, published online ahead of print January 22, 2001
School of Biological Sciences, College of Natural Sciences, Seoul National University, Seoul 151-742
Corresponding Author: depark{at}snu.ac.kr
Pix, a Pak-interacting exchange factor is known to be involved in the regulation of Cdc42/Rac GTPases. The 85-kDa
J. Biol. Chem, 10.1074/jbc.C000806200
Submitted on November 14, 2000
Revised on January 16, 2001
Accepted on January 22, 2001
Leucine zipper-mediated homodimerization of the Pak kinase interacting factor,
Pix: Implication for a role in cytoskeletal reorganization
Pix-a protein contains a SH3 domain, the tandem DH and PH domain, a proline-rich region and a GIT1-binding domain. In addition to those domains, Pix-a also contains a putative leucine zipper domain at the carboxyl terminal end. In this study, we demonstrate that the previously identified putative leucine zipper domain mediates the formation of Pix-a homodimers. Using in vitro and in vivo methodologies, we show that deletion of the leucine zipper domain is sufficient to abolish Pix-a homodimerization. In NIH3T3 fibroblast cells, expression of wild type Pix-a induces the formation of membrane ruffles. However, cells expressing the leucine zipper domain-deletion mutant could not form membrane ruffle structures. Moreover, PDGF-mediated cytoskeletal changes were completely blocked by the leucine zipper domain-deletion mutant. The results suggest that the leucine zipper domain enables Pix-a to homodimerize, and homodimerization is essential for Pix-a signaling functions leading to the cytoskeletal reorganization.
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