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Originally published In Press as doi:10.1074/jbc.M208949200 on October 21, 2002

J. Biol. Chem., Vol. 278, Issue 1, 545-555, January 3, 2003
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Heterodimerization of Endothelin-converting Enzyme-1 Isoforms Regulates the Subcellular Distribution of This Metalloprotease*

Laurent MullerDagger , Alain Barret, Eric Etienne, Rina Meidan§, Olivier Valdenaire, Pierre Corvol, and Claude Tougard

From the INSERM U 36 Collège de France Paris, 75005 Paris, France

Endothelin-converting enzyme (ECE) is a membrane metalloprotease that generates endothelin from its direct precursor big endothelin. Four isoforms of ECE-1 are produced from a single gene through the use of alternate promoters. These isoforms share the same extracellular catalytic domain and contain unique cytosolic tails, which results in their specific subcellular targeting. We investigated the distribution of ECE-1 isoforms in transfected AtT-20 neuroendocrine cells. Whereas ECE-1a and 1c were present at the plasma membrane, ECE-1b and ECE-1d were retained inside the cells. We found that both intracellular isoforms were concentrated in the endosomal system: ECE-1d in recycling endosomes, and ECE-1b in late endosomes/multivesicular bodies. Leucine-based motifs were involved in the intracellular retention of these isoforms, and the targeting of ECE-1b to the degradation pathway required an additional signal in the N terminus. The concentration of ECE-1 isoforms in the endosomal system suggested new functions for these enzymes. Potential novel functions include redistribution of other isoforms through direct interaction. We have showed that ECE-1 isoforms could heterodimerize, and that in such heterodimers the ECE-1b targeting signal was dominant. Interaction of a plasma membrane isoform with ECE-1b resulted in its intracellular localization and decreased its extracellular activity. These data demonstrated that the targeting signals specific for ECE-1b constitute a regulatory domain per se that could modulate the localization and the activity of other isoforms.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: INSERM U36, Collège de France, 11 Place M.Berthelot, 75005 Paris, France. Tel: 33-1-44-27-14-29; Fax: 33-1-44-27-16-91; E-mail: laurent.muller@college-de-france.fr.

§ Present address: Dept. of Animal Science, Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, Rehovot 76100, Israel.

Present address: AXOVAN AG, Gewerbestrasse 16, 4123 Allschwil, Switzerland.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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