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Vol. 11, Issue 10, 3629-3643, October 2000
Department of Molecular Genetics, Weizmann Institute of Science,
Rehovot 76100, Israel
In yeast, homologues of the synaptobrevin/VAMP family of v-SNAREs
(Snc1 and Snc2) confer the docking and fusion of secretory vesicles at
the cell surface. As no v-SNARE has been shown to confer endocytosis,
we examined whether yeast lacking the SNC genes, or
possessing a temperature-sensitive allele of SNC1
(SNC1ala43), are deficient in the endocytic
uptake of components from the cell surface. We found that both
SNC and temperature-shifted
SNC1ala43 yeast are deficient in their
ability to deliver the soluble dye FM4-64 to the vacuole. Under
conditions in which vesicles accumulate, FM4-64 stained primarily the
cytoplasm as well as fragmented vacuoles. In addition,
-factor-stimulated endocytosis of the -factor receptor, Ste2,
was fully blocked, as evidenced using a Ste2-green fluorescent protein
fusion protein as well as metabolic labeling studies. This suggests a
direct role for Snc v-SNAREs in the retrieval of membrane proteins from
the cell surface. Moreover, this idea is supported by genetic and
physical data that demonstrate functional interactions with t-SNAREs
that confer endosomal transport (e.g., Tlg1,2). Notably,
Snc1ala43 was found to be nonfunctional in cells lacking
Tlg1 or Tlg2. Thus, we propose that synaptobrevin/VAMP family members
are engaged in anterograde and retrograde protein sorting steps between
the Golgi and the plasma membrane.
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