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Originally published In Press as doi:10.1074/jbc.M204554200 on June 20, 2002

J. Biol. Chem., Vol. 277, Issue 35, 31679-31693, August 30, 2002
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Regulation of the Human Cyclin-dependent Kinase Inhibitor p18INK4c by the Transcription Factors E2F1 and Sp1*

Alexandre BlaisDagger , Didier Monté§, Frédéric PouliotDagger , and Claude LabrieDagger

From the Dagger  Molecular Endocrinology and Oncology Research Center, Centre Hospitalier de l'Université Laval Research Center, Centre Hospitalier Universitaire de Quebec, Sainte-Foy, G1V 4G2 Quebec, Canada and § Formation de Recherche en Evolution No. 2527, Institut de Biologie de Lille, 59021 Lille Cedex, France

The p18INK4c cyclin-dependent kinase inhibitor is an important regulator of cell cycle progression and cellular differentiation. We and others found that overexpressed E2F proteins up-regulate p18 expression. To better understand this phenomenon, we performed a functional analysis of the human p18 promoter. Deletion studies revealed that the E2F-responsive elements of the promoter are located within 131 bp upstream of the transcription start site. This region contains putative Sp1- and E2F-binding sites. Mutational inactivation of these elements revealed that the Sp1 sites were important for the basal activity of the promoter but could also mediate the effects of E2F1 on the p18 promoter. Moreover, we found that E2F1 and Sp1 can synergistically enhance the activity of the proximal p18 promoter. Gel shift analyses using p18 promoter-derived probes led to the identification of several multiprotein complexes that were found to contain different combinations of E2F proteins and/or Sp1. Recombinant E2F1 was also capable of binding to the E2F-binding sites. Chromatin immunoprecipitation experiments demonstrated that E2F1 and E2F4 associate with the p18 promoter in unperturbed cells. Based on these findings, we conclude that E2F proteins and Sp1 play an important role in the control of p18 expression.

* This work was supported in part by fellowships from the Fonds de la Recherche en Santé du Québec (to A. B., F. P., and C. L.), by the Canadian Medical Research Council (to D. M.), by the Association pour la Recherche sur le Cancer (to D. M.), and by EndoRecherche.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.

To whom correspondence should be addressed. Tel.: 418-654-2296; Fax: 418-654-2761; E-mail: Claude.Labrie@crchul.ulaval.ca.

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


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