title: Pumping lipids with P4-ATPases.
abstract: While accumulating evidence indicates that P4-ATPases catalyze phospholipid transport across cellular bilayers, their kinship to cation-pumping ATPases has raised fundamental questions concerning the underlying flippase mechanism. Loss of P4-ATPase function perturbs vesicle formation in late secretory and endocytic compartments. An intriguing concept is that P4-ATPases help drive vesicle budding by generating imbalances in transbilayer lipid numbers. Moreover, activation of P4-ATPases by phosphoinositides and other effectors of coat recruitment provide a potential mechanism to confine flippase activity to sites of vesicle biogenesis. These developments have raised considerable interest in understanding the mechanism, regulation and biological implications of P4-ATPase-catalyzed phospholipid transport.
authors.affiliation: Center for Membrane Pumps in Cells and Disease-PUMPKIN, Danish National Research Foundation, Department of Plant Biology and Biotechnology, Faculty of Life Sciences, University of Copenhagen, Frederiksberg C, Copenhagen, Denmark.
authors.forename: Rosa L
authors.initials: RL
authors.lastname: López-Marqués
authors.forename: Joost C M
authors.initials: JC
authors.lastname: Holthuis
authors.forename: Thomas G
authors.initials: TG
authors.lastname: Pomorski
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001692:Biological Transport; D008055:Lipids / Q000502:physiology*; D008954:Models, Biological
chemical_list: D008055:Lipids; D000251:Adenosine Triphosphatases