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J. Biol. Chem., Vol. 277, Issue 28, 24859-24862, July 12, 2002
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2*
,
,
From the Institut de Génétique et de Biologie
Moléculaire et Cellulaire,
CNRS/INSERM/Université Louis
Pasteur/Collège de France, BP 163, 67404 Illkirch Cedex, France and Nuclear retinoic acid (RA) receptors (RARs) are
phosphorylated at conserved serine residues located in their N-terminal
domain. Phosphorylation of RAR Laboratorio di Biologia Molecolare,
Istituto di Ricerche Farmacologiche Mario Negri, Via Eritrea 62, 20157 Milano, Italia
2 at these residues is increased in
response to RA subsequently to the activation of p38MAPK. We show here that this RA-induced phosphorylation of RAR2 resulted from
the down-regulation of the phosphatidylinositol 3-kinase (PI3K)/Akt pathway. By overexpressing Akt and by using agents that activated or
inhibited the PI3K/Akt pathway, we also demonstrated that the RA-induced down-regulation of the PI3K/Akt pathway targeted not only
the phosphorylation of RAR2 but also the turnover and
transcriptional activity of the receptor. Altogether these data
indicate that the PI3K/Akt pathway plays an important role in retinoic
acid signaling.
Supported by short term fellowships from the Human Frontier
Science Program, by the Association pour la Recherche sur le Cancer, and by FIRC (Fondazione Italiana per la Ricerca sul Cancro). Present address: Laboratorio di Biologia Molecolare, Istituto di Ricerche Farmacologiche Mario Negri, Via Eritrea 62, 20157 Milano, Italia.
§
Supported by Fondation Chateaubriand and by an INSERM fellowship.
Present address: Sigma Israël, Plaut 3, Park-Rabin, Rehovot, Israël 76100.
¶
Supported by the Ministère de la Recherche et de
l'Enseignement Supérieur.
**
To whom correspondence should be addressed: Institut de
Génétique et de Biologie Moléculaire et Cellulaire,
BP 163, 67404 Illkirch Cedex, Communauté Urbaine de
Strasbourg, France. Tel.: 33-3-88-65-34-59; Fax: 33-3-88-65-32-01;
E-mail: cegly@igbmc.u-strasbg.fr.
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