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Vol. 12, Issue 3, 711-723, March 2001
Institut für Mikrobiologie, Heinrich-Heine-Universität
Düsseldorf, D-40225 Düsseldorf, Germany
The multispanning membrane protein Ste6, a member of the
ABC-transporter family, is transported to the yeast vacuole for
degradation. To identify functions involved in the intracellular
trafficking of polytopic membrane proteins, we looked for functions
that block Ste6 transport to the vacuole upon overproduction. In our
screen, we identified several known vacuolar protein sorting
(VPS) genes (SNF7/VPS32,
VPS4, and VPS35) and a previously
uncharacterized open reading frame, which we named MOS10
(more of Ste6). Sequence analysis showed that Mos10 is a member of a
small family of coiled-coil-forming proteins, which includes Snf7 and
Vps20. Deletion mutants of all three genes stabilize Ste6 and show a
"class E vps phenotype." Maturation of the vacuolar
hydrolase carboxypeptidase Y was affected in the mutants and the
endocytic tracer FM4-64 and Ste6 accumulated in a dot or ring-like
structure next to the vacuole. Differential centrifugation experiments
demonstrated that about half of the hydrophilic proteins Mos10 and
Vps20 was membrane associated. The intracellular distribution was
further analyzed for Mos10. On sucrose gradients, membrane-associated
Mos10 cofractionated with the endosomal t-SNARE Pep12, pointing to an
endosomal localization of Mos10. The growth phenotypes of the mutants
suggest that the "Snf7-family" members are involved in a
cargo-specific event.
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