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Nucleic Acids Research, 2002, Vol. 30, No. 8 1789-1798
© 2002 Oxford University Press

Binding of USF to a non-canonical E-box following stress results in a cell-specific derepression of the lama3 gene

Thierry Virolle, Christelle Coraux, Olivier Ferrigno, Laurence Cailleteau, Jean-Paul Ortonne, Philippe Pognonec1 and Daniel Aberdam*

U385 INSERM, Faculté de Médecine, 06107 Nice Cedex 2, France and 1Institute of Signaling, Developmental Biology and Cancer Research, Centre de Biochimie, Parc Valrose, 06108 Nice Cedex 2, France

Expression of the lama3 gene, encoding the laminin {alpha}3A chain, is restricted to specialized epithelia. We previously showed that lama3 gene expression is controlled by an epithelial enhancer through the cooperative effect of AP-1 binding sites. In fibroblasts, there is no lama3 expression because of the recruitment of a repressor complex absent or inactive in epithelial cells. In this paper, we show evidence that this repression of the lama3 gene is relieved by exogenous and UV-induced USF-1 through its interaction with a non-canonical E-box site. Using a chromatin immunoprecipitation assay, we find that UV stress induces USF to bind to the lama3 promoter in vivo. We further demonstrate that this loss of cell specificity is directly related to the accessibility of the E-box, resulting in a strong induction in fibroblasts, while expression remains constitutively high in keratinocytes. This accessibility appears to be dependent upon the recruitment of a fibroblastic repressor complex. Therefore, we speculate that anchorage of this repressor complex in fibroblasts modifies the enhancer geometry, allowing USF to interact under stress-inducing conditions with its heptameric binding site.

* To whom correspondence should be addressed. Tel: +33 4 93 37 77 18; Fax: +33 4 93 81 14 04; Email: aberdam{at}unice.fr


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