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First published online 18 March 2003
doi: 10.1242/jcs.00395
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Research Article |
1 Department of Molecular, Cellular and Developmental Biology, University of
Colorado, Campus Box 347, Boulder, CO 80309, USA
2 Department of Cellular and Molecular Medicine, Howard Hughes Medical
Institute, Campus Box 0668, School of Medicine, University of California, San
Diego, La Jolla, CA 92093, USA
Present address: Department of Biochemistry and Molecular Biology, 1611
Guggenheim Building, Mayo Clinic, Rochester, MN 55902, USA
Present address: Microgenomics, 5935 Darwin Court, Carlsbad, CA 92008,
USA
* Author for correspondence (e-mail: odorizzi{at}colorado.edu)
Accepted 28 January 2003
Multivesicular bodies are late endosomal compartments containing lumenal vesicles that are formed by inward budding of the limiting endosomal membrane. In the yeast Saccharomyces cerevisiae, integral membrane proteins are sorted into the lumenal vesicles of multivesicular bodies, and this process requires the class E subset of VPS genes. We show that one of the class E VPS genes, BRO1/VPS31, encodes a cytoplasmic protein that associates with endosomal compartments. The dissociation of Bro1 from endosomes requires another class E Vps protein, Vps4, which is an ATPase that also regulates the endosomal dissociation of ESCRT-III, a complex of four class E Vps proteins (Vps2, Vps20, Vps24 and Snf7/Vps32) that oligomerize at the endosomal membrane. We also show that the endosomal association of Bro1 is specifically dependent on one of the ESCRT-III components, Snf7. Our data suggest that the function of Bro1 in the MVB pathway takes place on endosomal membranes and occurs in concert with or downstream of the function of the ESCRT-III complex.
Key words: Multivesicular, Vesicle, Transport, Vacuole
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