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Vol. 10, Issue 6, 1719-1732, June 1999
Institute of Molecular Biology, University of Oregon, Eugene,
Oregon 97403-1229
The interaction between v-SNAREs on transport vesicles and t-SNAREs
on target membranes is required for membrane traffic in eukaryotic
cells. Here we identify Vti1p as the first v-SNARE protein found to be
required for biosynthetic traffic into the yeast vacuole, the
equivalent of the mammalian lysosome. Certain vti1-ts
yeast mutants are defective in alkaline phosphatase transport from the
Golgi to the vacuole and in targeting of aminopeptidase I from the cytosol to the vacuole. VTI1 interacts
genetically with the vacuolar t-SNARE VAM3, which is
required for transport of both alkaline phosphatase and
aminopeptidase I to the vacuole. The v-SNARE Nyv1p
forms a SNARE complex with Vam3p in homotypic vacuolar fusion; however,
we find that Nyv1p is not required for any of the three biosynthetic
pathways to the vacuole. v-SNAREs were thought to ensure specificity in
membrane traffic. However, Vti1p also functions in two additional
membrane traffic pathways: Vti1p interacts with the t-SNAREs Pep12p in
traffic from the TGN to the prevacuolar compartment and with Sed5p in
retrograde traffic to the cis-Golgi. The ability of
Vti1p to mediate multiple fusion steps requires additional proteins to
ensure specificity in membrane traffic.
Corresponding author. E-mail address:
stevens{at}molbio.uoregon.edu.
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