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J. Cell Biol.,
Volume 142, Number 3, August 10, 1998 651-663
* Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403-1229; A large number of trafficking steps occur between the last compartment of the Golgi apparatus
(TGN) and the vacuole of the yeast Saccharomyces cerevisiae. To date, two intracellular routes from the TGN
to the vacuole have been identified. Carboxypeptidase Y (CPY) travels through a prevacuolar/endosomal
compartment (PVC), and subsequently on to the vacuole, while alkaline phosphatase (ALP) bypasses this
compartment to reach the same organelle. Proteins resident to the TGN achieve their localization despite a
continuous flux of traffic by continually being retrieved
from the distal PVC by virtue of an aromatic amino
acid-containing sorting motif. In this study we report
that a hybrid protein based on ALP and containing this
retrieval motif reaches the PVC not by following the
CPY sorting pathway, but instead by signal-dependent
retrograde transport from the vacuole, an organelle
previously thought of as a terminal compartment. In
addition, we show that a mutation in VAC7, a gene
previously identified as being required for vacuolar inheritance, blocks this trafficking step. Finally we show
that Vti1p, a v-SNARE required for the delivery of
both CPY and ALP to the vacuole, uses retrograde
transport out of the vacuole as part of its normal cellular itinerary.
Department of Physiology, University of
Iowa, Iowa City, Iowa 52242; and § Department of Biochemistry, University of Iowa, Iowa City, Iowa 52242
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