The transport mechanism of P4 ATPase lipid flippases

被引:28
|
作者
Lopez-Marques, Rosa L. [1 ]
Gourdon, Pontus [2 ,3 ]
Pomorski, Thomas Guenther [1 ,4 ]
Palmgren, Michael [1 ]
机构
[1] Univ Copenhagen, Dept Plant & Environm Sci, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
[2] Univ Copenhagen, Dept Biomed Sci, Blegdamsvej 3B, DK-2200 Copenhagen N, Denmark
[3] Lund Univ, Dept Expt Med Sci, Solvegatan 19, S-22184 Lund, Sweden
[4] Ruhr Univ, Fac Chem & Biochem, Dept Mol Biochem, Bochum, Germany
关键词
INTRAHEPATIC CHOLESTASIS TYPE-1; HIGHLY CONSERVED RESIDUES; YEAST PLASMA-MEMBRANE; PHOSPHOLIPID FLIPPASE; BETA-SUBUNIT; AMINOPHOSPHOLIPID TRANSLOCASE; SUBCELLULAR-LOCALIZATION; FUNCTIONAL-ROLE; CDC50; PROTEINS; GOLGI-COMPLEX;
D O I
10.1042/BCJ20200249
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
P4 ATPase lipid flippases are ATP-driven transporters that translocate specific lipids from the exoplasmic to the cytosolic leaflet of biological membranes, thus establishing a lipid gradient between the two leaflets that is essential for many cellular processes. While substrate specificity, subcellular and tissue-specific expression, and physiological functions have been assigned to a number of these transporters in several organisms, the mechanism of lipid transport has been a topic of intense debate in the field. The recent publication of a series of structural models based on X-ray crystallography and cryo-EM studies has provided the first glimpse into how P4 ATPases have adapted the transport mechanism used by the cation-pumping family members to accommodate a substrate that is at least an order of magnitude larger than cations.
引用
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页码:3769 / 3790
页数:22
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