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J Biol Chem, Vol. 273, Issue 5, 2624-2630, January 30, 1998
From the Institute of Molecular Biology, University of Oregon,
Eugene, Oregon 97403-1229
Membrane traffic in eukaryotic cells requires the
interaction of a vesicle-associated soluble NSF attachment protein
receptor (v-SNARE) on transport vesicles with a SNARE on the target
membrane (t-SNARE). Recently, we identified the yeast protein Vti1p as a v-SNARE that is involved in two transport reactions. Vti1p interacts with the prevacuolar t-SNARE Pep12p in Golgi to prevacuolar transport and with the cis-Golgi t-SNARE Sed5p in traffic to the cis-Golgi. Here
we describe a human Vti1p homolog, hVti1. Whereas vti1
cells are inviable, expression of hVti1 allows vti1
cells to grow at nearly the wild-type growth rate. When expressed in
yeast hVti1 can replace Vti1p in both Golgi to prevacuolar transport
and in traffic to the cis-Golgi. Sequence comparisons with a
Schizosaccharomyces pombe and two different mouse Vti1
homologs led to the identification of a very conserved predicted
-helix. Amino acid exchanges in vti1 mutant alleles
defective either in one or both trafficking steps cluster in this
domain, suggesting that this structure is probably the binding site for
effector proteins.
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