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Licensed Unlicensed Requires Authentication Published by De Gruyter June 18, 2011

Pumping lipids with P4-ATPases

  • Rosa L. López-Marqués , Joost C.M. Holthuis EMAIL logo and Thomas G. Pomorski
From the journal Biological Chemistry


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.

Corresponding authors

Received: 2010-8-23
Accepted: 2010-11-11
Published Online: 2011-06-18
Published in Print: 2011-02-01

©2011 by Walter de Gruyter Berlin New York

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