1887

Abstract

Members of the SNARE protein family participate in the docking–fusion step of several intracellular vesicular transport events. Vam7p was identified as a SNARE protein that acts in vacuolar protein transport and membrane fusion. However, in , there have been no reports regarding the counterpart of Vam7p. Here, we found that, although the SPCC594.06c gene has low similarity to Vam7p, the product of SPCC594.06c has a PX domain and SNARE motif like Vam7p, and thus we designated the gene (am-ike protein 1). The Δ cells showed no obvious defect in vacuolar protein transport. However, cells of the Δ mutant with a deletion of , which encodes another SNARE protein, displayed extreme defects in vacuolar protein transport and vacuolar morphology. Vsl1p was localized to the vacuolar membrane and prevacuolar compartment, and its PX domain was essential for proper localization. Expression of the fusion protein GFP-Vsl1p was able to suppress ZnCl sensitivity and the vacuolar protein sorting defect in the Δ cells. Moreover, GFP-Vsl1p was mislocalized in a Δ mutant and in cells overexpressing . Importantly, overexpression of could suppress the sensitivity to ZnCl of Δ cells and the vacuolar morphology defect of ΔΔ cells in . Taken together, these data suggest that Vsl1p and Fsv1p are required for vacuolar protein transport and membrane fusion, and they function cooperatively with Pep12p in the same membrane-trafficking step.

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2015-01-01
2024-04-25
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