The transport mechanism of P4 ATPase lipid flippases
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The transport mechanism of P4 ATPase lipid flippases. / López-Marqués, Rosa L; Gourdon, Pontus; Günther Pomorski, Thomas; Palmgren, Michael.
In: Biochemical Journal, Vol. 477, No. 19, 2020, p. 3769-3790.Research output: Contribution to journal › Review › Research › peer-review
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TY - JOUR
T1 - The transport mechanism of P4 ATPase lipid flippases
AU - López-Marqués, Rosa L
AU - Gourdon, Pontus
AU - Günther Pomorski, Thomas
AU - Palmgren, Michael
N1 - © 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.
PY - 2020
Y1 - 2020
N2 - 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.
AB - 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.
U2 - 10.1042/BCJ20200249
DO - 10.1042/BCJ20200249
M3 - Review
C2 - 33045059
VL - 477
SP - 3769
EP - 3790
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 19
ER -
ID: 250132607