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J. Biol. Chem., Vol. 278, Issue 23, 21155-21161, June 6, 2003

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Enterophilin-1, a New Partner of Sorting Nexin 1, Decreases Cell Surface Epidermal Growth Factor Receptor^*

Véronique Pons , Françoise Hullin-Matsuda, Michel Nauze, Ronald Barbaras, Christine Pérès, Xavier Collet, Bertrand Perret, Hugues Chap and Ama Gassama-Diagne 

From the Institut Fédératif de Recherche Claude de Préval, IFR 30, Université Paul Sabatier, and Centre Hospitalo-Universitaire de Toulouse, INSERM Unité 563, Department of Lipoproteins and Lipid Mediators, Hôpital Purpan, F31059 Toulouse Cedex, France

We previously described enterophilin-1 (Ent-1), a new intestinal protein bearing an extended leucine zipper and a B30.2 domain. Ent-1 expression is associated with growth arrest and enterocyte differentiation. To investigate the importance of Ent-1 in the differentiation, we performed a yeast two-hybrid screening. We identified sorting nexin 1 (SNX1) as a novel partner of Ent-1 and confirmed the specificity of interaction by co-immunoprecipitation experiments in mammalian cells. SNX1 is associated with endosomal membranes and triggers the endosome-to-lysosome pathway of epidermal growth factor receptor (EGFR). We observe by immunofluorescence microscopy that Ent-1 and SNX1 are co-localized on vesicular and tubulovesicular structures, which are different from early endosome antigen 1-containing endosomes. By gel filtration chromatography, we show that Ent-1 and SNX1 co-eluted in macromolecular complexes containing part of EGFR. Furthermore, overexpressed Ent-1 decreases cell surface EGFR. Ent-1 and SNX1 co-overexpression strongly extends EGFR diminution, indicating a synergetic effect of both proteins on cell surface EGFR removal. Interestingly, the increase of endogenous Ent-1 expression correlates with the decrease of EGFR during spontaneous differentiation of Caco-2 cells. We thus propose a role of Ent-1 in the trafficking of EGFR to down-regulate intestinal mitogenic signals, highlighting the mechanisms of cell growth arrest associated with enterocytic differentiation.

Received for publication, October 28, 2002 , and in revised form, February 7, 2003.

^* This work was supported by a grant from l'Association pour la Recherche sur le Cancer and by the ARECA (Alliance des Recherches sur le Cancer) network "Proteomics and Cancer." 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.

Supported by fellowships from Ministère de l'Education Nationale, de la Recherche et de la Technologie and from La Ligue Nationale contre le Cancer.

To whom correspondence should be addressed: INSERM Unité 563, Bat C, Department of Lipoproteins and Lipid Mediators, Hôpital Purpan, 31059 Toulouse Cedex, France. Tel.: 33-5-61-77-94-00; Fax: 33-5-61-77-94-01; E-mail: Ama.Gassama{at}toulouse.inserm.fr.

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