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A more recent version of this article appeared on July 1, 2004
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Submitted on November 7, 2003
Revised on March 11, 2004
Accepted on April 9, 2004
1 Laboratoire de Transport et Compartimentation Intracellulaires, IBCP, UMR5086 CNRS, IFR128 BioSciences Lyon-Gerland, 7 Passage du Vercors, 69367 Lyon, France
2 Laboratoire de RMN et Bioinformatique Structurales, IBCP, UMR5086 CNRS, IFR128 BioSciences Lyon-Gerland, 7 Passage du Vercors, 69367 Lyon, France
3 Laboratoire de BioCristallographie, IBCP, UMR5086 CNRS, IFR128 BioSciences Lyon-Gerland, 7 Passage du Vercors, 69367 Lyon, France
4 Laboratoire Modèles Levure de Pathologies Humaines, IBMC, FRE2375 CNRS, 15 rue Descartes, 67084 Strasbourg, France
* Corresponding author. E-mail address: S.Friant{at}ibmc.u-strasbg.fr.
At the late endosomes, cargoes destined for the interior of the vacuole are sorted into invaginating vesicles of the multivesicular body. Both, PtdIns(3,5)P2 and ubiquitin are necessary for proper sorting of some of these cargoes. We show that Ent5p, a yeast protein of the epsin family homologous to Ent3p, localizes to endosomes and specifically binds to PtdIns(3,5)P2 via its ENTH domain. In cells lacking Ent3p and Ent5p, ubiquitin-dependent sorting of biosynthetic and endocytic cargo into the multivesicular body is disrupted, while other trafficking routes to the vacuole are not affected. Ent3p and Ent5p are associated with Vps27p, a FYVE domain containing protein that interacts with ubiquitinated cargoes and is required for protein sorting into the multivesicular body. Therefore, Ent3p and Ent5p are the first proteins shown to be connectors between PtdIns(3,5)P2- and the Vps27p-ubiquitin-driven sorting machinery at the multivesicular body.
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