The transport mechanism of P4 ATPase lipid flippases

Research output: Contribution to journal › Review › Research › peer-review

Standard

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

Harvard

López-Marqués, RL, Gourdon, P, Günther Pomorski, T & Palmgren, M 2020, 'The transport mechanism of P4 ATPase lipid flippases', Biochemical Journal, vol. 477, no. 19, pp. 3769-3790. https://doi.org/10.1042/BCJ20200249

APA

López-Marqués, R. L., Gourdon, P., Günther Pomorski, T., & Palmgren, M. (2020). The transport mechanism of P4 ATPase lipid flippases. Biochemical Journal, 477(19), 3769-3790. https://doi.org/10.1042/BCJ20200249

Vancouver

López-Marqués RL, Gourdon P, Günther Pomorski T, Palmgren M. The transport mechanism of P4 ATPase lipid flippases. Biochemical Journal. 2020;477(19):3769-3790. https://doi.org/10.1042/BCJ20200249

Author

López-Marqués, Rosa L ; Gourdon, Pontus ; Günther Pomorski, Thomas ; Palmgren, Michael. / The transport mechanism of P4 ATPase lipid flippases. In: Biochemical Journal. 2020 ; Vol. 477, No. 19. pp. 3769-3790.

Bibtex

@article{10b00d56795148bc9b3a9ad2d6df6ee9,
title = "The transport mechanism of P4 ATPase lipid flippases",
abstract = "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.",
author = "L{\'o}pez-Marqu{\'e}s, {Rosa L} and Pontus Gourdon and {G{\"u}nther Pomorski}, Thomas and Michael Palmgren",
note = "{\textcopyright} 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.",
year = "2020",
doi = "10.1042/BCJ20200249",
language = "English",
volume = "477",
pages = "3769--3790",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "19",

}

RIS

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