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Vol. 8, Issue 12, 2659-2676, December 1997
and
*Department of Molecular Biology, Princeton University, Princeton,
New Jersey 08544; and
The protein trafficking machinery of eukaryotic cells is employed
for protein secretion and for the localization of resident proteins of
the exocytic and endocytic pathways. Protein transit between organelles
is mediated by transport vesicles that bear integral membrane proteins
(v-SNAREs) which selectively interact with similar proteins on the
target membrane (t-SNAREs), resulting in a docked vesicle. A novel
Saccharomyces cerevisiae SNARE protein, which has been
termed Vti1p, was identified by its sequence similarity to known
SNAREs. Vti1p is a predominantly Golgi-localized 25-kDa type II
integral membrane protein that is essential for yeast viability. Vti1p
can bind Sec17p (yeast SNAP) and enter into a Sec18p (NSF)-sensitive
complex with the cis-Golgi t-SNARE Sed5p. This
Sed5p/Vti1p complex is distinct from the previously described Sed5p/Sec22p anterograde vesicle docking complex. Depletion of Vti1p in
vivo causes a defect in the transport of the vacuolar protein
carboxypeptidase Y through the Golgi. Temperature-sensitive mutants of
Vti1p show a similar carboxypeptidase Y trafficking defect, but the
secretion of invertase and gp400/hsp150 is not significantly affected.
The temperature-sensitive vti1 growth defect can be
rescued by the overexpression of the v-SNARE, Ykt6p, which physically
interacts with Vti1p. We propose that Vti1p, along with Ykt6p and
perhaps Sft1p, acts as a retrograde v-SNARE capable of interacting with
the cis-Golgi t-SNARE Sed5p.
Cellular Biochemistry and
Biophysics Program, Memorial Sloan-Kettering Cancer Center, New
York, New York 10021
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