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Vol. 14, Issue 3, 1240-1254, March 2003
¶
*Department of Membrane Enzymology, Center for
Biomembranes and Lipid Enzymology, Utrecht University, 3584 CH Utrecht,
The Netherlands; Plasma membranes in eukaryotic cells display asymmetric lipid
distributions with aminophospholipids concentrated in the inner and
sphingolipids in the outer leaflet. This asymmetry is maintained by
ATP-driven lipid transporters whose identities are unknown. The yeast
plasma membrane contains two P-type ATPases, Dnf1p and Dnf2p, with
structural similarity to ATPase II, a candidate aminophospholipid translocase from bovine chromaffin granules. Loss of Dnf1p and Dnf2p
virtually abolished ATP-dependent transport of NBD-labeled phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner plasma membrane leaflet, leaving transport of sphingolipid analogs unaffected. Labeling with trinitrobenzene sulfonic acid revealed that the amount of phosphatidylethanolamine exposed on the surface of Department of Cell Biology and
Histology, Academic Medical Center, 1105 AZ Amsterdam, The Netherlands;
Department of Biochemistry, University of
Geneva, Geneva CH-1211, Switzerland; and
§Institut de Biologie Physico-chimique, 75005 Paris, France
dnf1dnf2 cells increased
twofold relative to wild-type cells. Phosphatidylethanolamine exposure
by dnf1dnf2 cells further increased upon removal
of Drs2p, an ATPase II homolog in the yeast Golgi. These changes in
lipid topology were accompanied by a cold-sensitive defect in the
uptake of markers for bulk-phase and receptor-mediated
endocytosis. Our findings demonstrate a requirement for Dnf1p and Dnf2p
in lipid translocation across the yeast plasma membrane. Moreover, it
appears that Dnf1p, Dnf2p and Drs2p each help regulate the transbilayer
lipid arrangement in the plasma membrane, and that this regulation is
critical for budding endocytic vesicles.
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