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A more recent version of this article appeared on March 1, 2004
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Submitted on April 16, 2003
Revised on September 26, 2003
Accepted on October 24, 2003
1 Laboratoire de Neurogenèse et Morphogenèse au cours du Développement et chez l’Adulte (NMDA), UMR 6156 CNRS, IBDM, Université de la Méditerranée. Campus de Luminy, case 907. 13288 Marseille cedex 09. France, These authors have contributed equally to this work
2 Laboratoire de Neurogenèse et Morphogenèse au cours du Développement et chez l’Adulte (NMDA), UMR 6156 CNRS, IBDM, Université de la Méditerranée. Campus de Luminy, case 907. 13288 Marseille cedex 09. France
* Corresponding author. E-mail address: lebivic{at}ibdm.univ-mrs.fr.
Crumbs is an apical transmembrane protein crucial for epithelial morphogenesis in Drosophila melanogaster embryos. A protein with all the characteristics for a Crumbs homologue has been identified from patients suffering from Retinitis pigmentosa (RP12) but this protein (CRB1) is only expressed in retina and some parts of the brain both in human and mouse (den Hollander et al., 2002). Here, we describe CRB3, another Crumbs homologue that is preferentially expressed in epithelial tissues and skeletal muscles in human. CRB3 shares the conserved cytoplasmic domain with other Crumbs but exhibits a very short extracellular domain without the EGF- and laminin A-like G repeats present in the other Crumbs. CRB3 is localized to the apical and subapical area of epithelial cells from the mouse and human intestine, suggesting that it could play a role in epithelial morphogenesis. Indeed, expression of CRB3 or of a chimera containing the extracellular domain of the neurotrophin receptor p75NTR and the transmembrane and cytoplasmic domains of CRB3, led to a slower development of functional tight junctions in MDCK cells. This phenotype relied on the presence of CRB3 four last amino acids (ERLI) that are involved in a direct interaction with Par6, a regulator of epithelial polarity and tight junction formation. Thus CRB3, through its cytoplasmic domain and its interactors, plays a role in apical membrane morphogenesis and tight junction regulation.
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