Pumping lipids with P4-ATPases

TY - JOUR

T1 - Pumping lipids with P4-ATPases

AU - Lopez Marques, Rosa Laura

AU - C.M. Holthuis, Joost

AU - Günther-Pomorski, Thomas

PY - 2011/1/1

Y1 - 2011/1/1

N2 - 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.

AB - 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.

U2 - 10.1515/bc.2011.015

DO - 10.1515/bc.2011.015

M3 - Journal article

C2 - 21194369

SN - 1431-6730

VL - 392

SP - 67

EP - 76

JO - Biological Chemistry

JF - Biological Chemistry

IS - 1-2

ER -