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J. Biol. Chem., Vol. 278, Issue 21, 18859-18867, May 23, 2003

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ERK and p38 Inhibit the Expression of 4E-BP1 Repressor of Translation through Induction of Egr-1^*

Malvyne Rolli-Derkinderen , François Machavoine , Jay M. Baraban , Annabelle Grolleau ¶, Laura Beretta ¶ and Michel Dy  ||

From the CNRS FRE 2444, Université René Descartes Paris V, Hôpital Necker, Institut Federatif de Recherche Necker Enfants Malades, 75015 Paris, France, Department of Neurosciences, Psychiatry, and Behavioral Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, ^¶ Department of Microbiology and Immunology, University of Michigan, Ann Arbor, Michigan 48109-0666

4E-BP1 plays a major role in translation by inhibiting cap-dependent translation initiation. Several reports have investigated the regulation of 4E-BP1 phosphorylation, which varies along with cell differentiation and upon various stimulations, but very little is known about the regulation of its expression. In a first part, we show that the expression of 4E-BP1 protein and transcript decreases in hematopoietic cell lines cultivated in the presence of phorbol 12-myristate 13-acetate (PMA). This decrease depends on the activation of the ERK/mitogen-activated protein kinases. 4E-BP1 expression also decreases when the p38/mitogen-activated protein kinase pathway is activated by granulocyte/macrophage colony-stimulating factor but to a lesser extent than with PMA. In a second part, we examine how 4e-bp1 promoter activity is regulated. PMA and granulocyte/macrophage colony-stimulating factor induce Egr-1 expression through ERK and p38 activation, respectively. Using a dominant negative mutant of Egr, ZnEgr, we show that this transcription factor is responsible for the inhibition of 4e-bp1 promoter activity. In a third part we show that histidine decarboxylase, whose activity and expression are inversely correlated with 4E-BP1 expression, is a potential target for the translational machinery. These data (i) are the first evidence of a new role of ERK and p38 on the translational machinery and (ii) demonstrate that 4E-BP1 is a new target for Egr-1.

Received for publication, November 18, 2002 , and in revised form, February 27, 2003.

^|| To whom correspondence should be addressed: 161 rue de Sevres, 75743 Paris, Cedex 15, France. E-mail: dy{at}necker.fr.

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