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A more recent version of this article appeared on July 1, 2004
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Submitted on October 22, 2003
Revised on April 5, 2004
Accepted on April 7, 2004
1 Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor MI, 48109-0606; Department of Medical Biochemistry, University and Biocenter of Vienna, Austria
2 Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor MI, 48109-0606; Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143
3 Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor MI, 48109-0606
4 Department of Pharmacology, Wayne State University School of Medicine, Detroit MI, 48201; Department of Molecular and Integrative Physiology, University of Michigan Medical Center, Ann Arbor MI, 48109-0622
5 Departement de Biologie Cellulaire et Moleculaire, CEA Saclay, Gif-sur-Yvette 91191 Cedex, France
6 Departement de Biologie Cellulaire et Moleculaire, CEA Saclay, Gif-sur-Yvette 91191 Cedex, France; Dynamique de la Compartimentation Cellulaire, Institut des Sciences du Vègètal, CNRS UPR2355, Gif-sur-Yvette, France, & Epigenomics Project/genopole®, Evry, France
* Corresponding author. E-mail address: bfuller{at}umich.edu.
SOI3 was identified by a mutation, soi3-1, that suppressed a mutant TGN localization signal in the Kex2p cytosolic tail. SOI3, identical to RAV1, encodes a protein important for regulated assembly of vacuolar ATPase. Here we show that Soi3/Rav1p is required for transport between the early endosome and the late endosome/prevacuolar compartment (PVC). By EM, soi3-1 mutants massively accumulated structures that resembled early endosomes. soi3
mutants exhibited a kinetic delay in transfer of the endocytic tracer dye, FM4-64, from the 14°C endocytic intermediate to the vacuole. The soi3 mutation delayed vacuolar degradation but not internalization of the a-factor receptor, Ste3p. By density gradient fractionation, Soi3/Rav1p associated as a peripheral protein with membranes of a density characteristic of early endosomes. The soi3 null mutation markedly reduced the rate of Kex2p transport from the TGN to the PVC but had no effect on vacuolar protein sorting or cycling of Vps10p. These results suggest that assembly of vacuolar ATPase at the early endosome is required for transport of both Ste3p and Kex2p from the early endosome to the PVC and support a model in which cycling through the early endosome is part of the normal itinerary of Kex2p and other TGN resident proteins.
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