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Vol. 8, Issue 11, 2307-2327, November 1997
Department of Biology, Division of Cellular and Molecular Medicine,
Howard Hughes Medical Institute, University of California, San Diego,
School of Medicine, La Jolla, California 92093-0668
Protein transport to the lysosome-like vacuole in yeast is mediated
by multiple pathways, including the biosynthetic routes for vacuolar
hydrolases, the endocytic pathway, and autophagy. Among the more than
40 genes required for vacuolar protein sorting (VPS) in
Saccharomyces cerevisiae, mutations in the four class C
VPS genes result in the most severe vacuolar protein
sorting and morphology defects. Herein, we provide complementary
genetic and biochemical evidence that the class C VPS
gene products (Vps18p, Vps11p, Vps16p, and Vps33p) physically and
functionally interact to mediate a late step in protein transport to
the vacuole. Chemical cross-linking experiments demonstrated that
Vps11p and Vps18p, which both contain RING finger zinc-binding domains,
are components of a hetero-oligomeric protein complex that includes
Vps16p and the Sec1p homologue Vps33p. The class C Vps protein complex
colocalized with vacuolar membranes and a distinct dense membrane
fraction. Analysis of cells harboring a temperature-conditional
vps18 allele (vps18tsf) indicated
that Vps18p function is required for the biosynthetic, endocytic, and
autophagic protein transport pathways to the vacuole. In addition,
vps18tsf cells accumulated multivesicular
bodies, autophagosomes, and other membrane compartments that appear to
represent blocked transport intermediates. Overproduction of either
Vps16p or the vacuolar syntaxin homologue Vam3p suppressed defects
associated with vps18tsf mutant cells,
indicating that the class C Vps proteins and Vam3p may functionally
interact. Thus we propose that the class C Vps proteins are components
of a hetero-oligomeric protein complex that mediates the delivery of
multiple transport intermediates to the vacuole.
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