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Originally published In Press as doi:10.1074/jbc.M111284200 on January 18, 2002

J. Biol. Chem., Vol. 277, Issue 13, 11375-11384, March 29, 2002
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bcn-1 Element-dependent Activation of the Laminin gamma 1 Chain Gene by the Cooperative Action of Transcription Factor E3 (TFE3) and Smad Proteins*

Yasunobu KawataDagger , Hideaki SuzukiDagger , Yuji Higaki, Oleg Denisenko, Daniel Schullery, Christine Abrass, and Karol Bomsztyk§

From the Department of Medicine, Division of Nephrology, University of Washington, Seattle, Washington 98195

Laminin is a major component of the extracellular matrix. The laminin gamma 1 chain is the least variant component of the laminin heterotrimeric assembly. The laminin gamma 1 chain gene (LAMC1) expression is induced by several factors, including transforming growth factor-beta (TGF-beta ). LAMC1 promoter contains a highly conserved transcriptional element, bcn-1. We screened cDNA libraries with the yeast one-hybrid system to identify transcriptional factors that are recognized by the bcn-1 motif. Using this strategy we isolated the basic helix-loop-helix/leucine zipper (bHLHzip) E-box-binding transcription factor, TFE3. Until now, the E-box was the only element known to recruit the bHLHzip transcription factors. Although the bcn-1 element only remotely resembles the E-box sequence, we show that TFE3 binds and activates the bcn-1 element. TFE3 cooperates with Smad proteins in the activation of the LAMC1 promoter in cells, an effect that is critically dependent not only on the bcn-1 element but also on one of the Smad-binding elements (SBE). The cooperative induction of the LAMC1 promoter and the endogenous LAMC1 gene by TFE3 and Smad3 is augmented by the TGF-beta signaling pathway. Thus, the bcn-1 is a novel TFE3-dependent TGF-beta target element that regulates LAMC1 gene expression.

* This work was supported in part by National Institutes of Health Grants DK45978 and GM45134 and the Northwest Kidney Foundation (to K. B.) and by a grant from the American Heart Association Northwest Affiliate (to O. D.).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 Supported by a postdoctoral fellowship from the American Heart Association Northwest Affiliate.

§ To whom correspondence should be addressed: Dept. of Medicine, Box 356521, University of Washington, Seattle, WA 98195. Tel.: 206-543-3792; Fax: 206-685-8661; E-mail karolb@u.washington.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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