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J. Biol. Chem., Vol. 279, Issue 10, 9270-9277, March 5, 2004

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Enterophilin-1 Interacts with Focal Adhesion Kinase and Decreases ₁ Integrins in Intestinal Caco-2 Cells^*

Véronique Pons, Christine Pérès, Jeanne-Marie Teulié, Michel Nauze, Marianne Mus, Corinne Rolland, Xavier Collet, Bertrand Perret, Ama Gassama-Diagne, and Françoise Hullin-Matsuda

From the Institut Fédératif de Recherche Claude de Préval, IFR30, INSERM Unité 563, Département Lipoprotéines et Médiateurs Lipidiques, Hôpital Purpan, 31059 Toulouse Cedex, France

Intestinal cell growth and differentiation are tightly regulated by growth factors and extracellular matrix components along the crypt-villus axis. We previously described enterophilin-1 (Ent-1) as a new intestinal protein associated with growth arrest and enterocyte differentiation. Ent-1 interacted with sorting nexin 1 and decreased cell surface epidermal growth factor receptor. Because ₁ integrins are mostly found in vivo in the proliferative crypt cells, we investigated the role of Ent-1 in the fate of ₁ integrin subunits. In undifferentiated intestinal Caco-2 cells, overexpression of Ent-1 induces a marked decrease of ₅₁ integrin pools, whereas ₂₁ integrin is weakly affected. Conversely, overexpression of sorting nexin 1 has no effect on integrin levels despite its ability to interact with Ent-1. Interestingly, we identified focal adhesion kinase as a new Ent-1 partner using yeast two-hybrid screening and co-precipitation experiments. Furthermore by confocal microscopy, we observed that Ent-1 and ₁ integrins partly co-localize on vesicular structures, suggesting a role for Ent-1 in integrin trafficking. Because focal adhesion kinase is able to bind both Ent-1 and ₁ integrins, the kinase might act as a molecular bridge between the two proteins. Altogether, these results support a role of Ent-1 in regulating ₁ integrin expression that could favor intestinal differentiation.

Received for publication, September 3, 2003 , and in revised form, November 12, 2003.

^* This work was supported by a grant from L'Association pour la Recherche sur le Cancer and by the Alliances 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 the 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: Present address: RIKEN Frontier Research System, Supra-Biomolecular System Research Group, Sphingolipid Functions Laboratory 2-1, Hirosawa, Wakoshi, Saitama 351-0198, Japan. Tel.: 81-48-467-9628; Fax: 81-48-467-9626; E-mail: hullin-matsuda{at}riken.jp.

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