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MBC in Press, published online ahead of print July 16, 2002
Mol. Biol. Cell 10.1091/mbc.E02-03-0172

A more recent version of this article appeared on September 1, 2002
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Submitted on March 28, 2002
Revised on May 23, 2002
Accepted on June 5, 2002

An Essential Subfamily of Drs2p-Related P-Type ATPases are Required for Protein Trafficking between the Golgi Complex and the Endosomal/Vacuolar System

Zhaolin Hua1, Parvin Fatheddin1, and Todd R. Graham1*

1 Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235-1634

* Corresponding author. E-mail address: tr.graham{at}vanderbilt.edu.

The Saccharomyces cerevisiae genome contains five genes encoding P-type ATPases that are potential aminophospholipid translocases (APTs); DRS2, NEO1, and three uncharacterized ORFs, which we have named DNF1, DNF2 and DNF3 for DRS2/NEO1 Family. NEO1 is the only essential gene in APT family and appears to be functionally distinct from the DRS2/DNF genes. The drs2{Delta} dnf1{Delta} dnf2{Delta} dnf3{Delta} 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 (TGN). 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{Delta} dnf1{Delta} mutant grows slowly, massively accumulates intracellular membranes, and exhibits a substantial defect in the transport of alkaline phosphatase (ALP) to the vacuole. Transport of carboxypeptidase Y (CPY) to the vacuole is also perturbed, but to a lesser extent. In addition, the dnf1{Delta} dnf2{Delta} dnf3{Delta} mutant exhibits a defect in recycling of GFP-Snc1p in the early endocytic - late secretory pathways. Drs2p and Dnf3p colocalize with the TGN marker Kex2p, while Dnf1p and Dnf2p appear 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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