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© The Rockefeller University Press, 0021-9525/1999/12/1223/ $5.00
The Journal of Cell Biology, Volume 147, Number 6, December 13, 1999 1223-1236

Original Article

Role for Drs2p, a P-Type ATPase and Potential Aminophospholipid Translocase, in Yeast Late Golgi Function

Chih-Ying Chena, Michael F. Ingrama, Peter H. Rosala, and Todd R. Grahama
a Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235

Correspondence to: Todd R. Graham, Department of Molecular Biology, Vanderbilt University, Nashville, TN 37235. Tel:(615) 343-1835 Fax:(615) 343-6707 E-mail:tr.graham{at}vanderbilt.edu.

ADP-ribosylation factor appears to regulate the budding of both COPI and clathrin-coated transport vesicles from Golgi membranes. An arf1{Delta} synthetic lethal screen identified SWA3/DRS2, which encodes an integral membrane P-type ATPase and potential aminophospholipid translocase (or flippase). The drs2 null allele is also synthetically lethal with clathrin heavy chain (chc1) temperature-sensitive alleles, but not with mutations in COPI subunits or other SEC genes tested. Consistent with these genetic analyses, we found that the drs2{Delta} mutant exhibits late Golgi defects that may result from a loss of clathrin function at this compartment. These include a defect in the Kex2-dependent processing of pro–{alpha}-factor and the accumulation of abnormal Golgi cisternae. Moreover, we observed a marked reduction in clathrin-coated vesicles that can be isolated from the drs2{Delta} cells. Subcellular fractionation and immunofluorescence analysis indicate that Drs2p localizes to late Golgi membranes containing Kex2p. These observations indicate a novel role for a P-type ATPase in late Golgi function and suggest a possible link between membrane asymmetry and clathrin function at the Golgi complex.

Key Words: adenosine diphosphate–ribosylation factor, aminophospholipid translocase, clathrin, DRS2, trans-Golgi network


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