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Vol. 13, Issue 9, 3162-3177, September 2002
Department of Biological Sciences, Vanderbilt University,
Nashville, Tennessee 37235-1634
The Saccharomyces cerevisiae genome contains five
genes encoding P-type ATPases that are potential aminophospholipid
translocases (APTs): DRS2, NEO1, and
three uncharacterized open reading frames that we have named
DNF1, DNF2, and DNF3 for
DRS2/NEO1 family. NEO1 is the only
essential gene in APT family and seems to be functionally distinct from
the DRS2/DNF genes. The drs2
dnf1 dnf2 dnf3
quadruple mutant is inviable, although any one member of this group can
maintain viability, indicating that there is a substantial functional
overlap between the encoded proteins. We have previously implicated
Drs2p in clathrin function at the trans-Golgi network.
In this study, we constructed strains carrying all possible viable
combinations of null alleles from this group and analyzed them for
defects in protein transport. The drs2 dnf1 mutant grows slowly, massively accumulates
intracellular membranes, and exhibits a substantial defect in the
transport of alkaline phosphatase to the vacuole. Transport of
carboxypeptidase Y to the vacuole is also perturbed, but to a lesser
extent. In addition, the dnf1 dnf2
dnf3 mutant exhibits a defect in recycling of
GFP-Snc1p in the early endocytic-late secretory pathways. Drs2p and
Dnf3p colocalize with the trans-Golgi network marker
Kex2p, whereas Dnf1p and Dnf2p seem to localize to the plasma membrane and late exocytic or early endocytic membranes. We propose that eukaryotes express multiple APT subfamily members to facilitate protein
transport in multiple pathways.
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