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J. Biol. Chem., Vol. 280, Issue 50, 41537-41545, December 16, 2005

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p300 Modulates ATF4 Stability and Transcriptional Activity Independently of Its Acetyltransferase Domain^*

Irina Lassot1, Emilie Estrabaud2, Stephane Emiliani, Monsef Benkirane, Richard Benarous3, and Florence Margottin-Goguet4

From the Institut Cochin, Department of Maladies Infectieuses, INSERM U567, CNRS UMR8104, University Rene Descartes Paris V, Bat G. Roussy, 27 Rue du Faubourg Saint Jacques, 75014 Paris and CNRS UPR 1142, Institut de Génétique Humaine, 34396 Montpellier, France

ATF4 plays a crucial role in the cellular response to stress and multiple stress responses pathways converge to the translational up-regulation of ATF4. ATF4 is a substrate of the SCF^TrCP ubiquitin ligase that binds to TrCP through phosphorylation on a DSGXXXS motif. We show here that ATF4 stability is also modulated by the histone acetyltransferase p300, which induces ATF4 stabilization by inhibiting its ubiquitination. Despite p300 acetylates ATF4, we found that p300-mediated ATF4 stabilization is independent of p300 catalytic activity, using either the inactive form of p300 or the acetylation mutant ATF4-K311R. ATF4 deleted of its p300 binding domain is no more stabilized by p300 nor recruited into nuclear speckles. In consequence of ATF4 stabilization, both p300 and the catalytically inactive enzyme increase ATF4 transcriptional activity.

Received for publication, May 13, 2005 , and in revised form, September 16, 2005.

^* This work was supported in part by grants from Agence Nationale de Recherches sur le SIDA, Sidaction, Association pour la Recherche sur le Cancer la Ligue Nationale Contre le Cancer, and the post-genome program from the French Ministry of Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Supported by CNRS, INSERM, la Ligue Nationale Contre le Cancer, and by the French Ministry of Education.

² Supported by the French Ministry of Education.

³ To whom correspondence may be addressed. Tel.: 33-1-40-51-65-71; Fax: 33-1-40-51-65-70; E-mail: benarous{at}cochin.inserm.fr.

⁴ To whom correspondence may be addressed. Tel.: 33-1-40-51-65-74; Fax: 33-1-40-51-65-70; E-mail: margottin-goguet{at}cochin.inserm.fr.

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