P4-ATPases: lipid flippases in cell membranes

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

P4-ATPases : lipid flippases in cell membranes. / Lopez Marques, Rosa Laura; Theorin, Lisa; Palmgren, Michael Broberg; Günther-Pomorski, Thomas.

In: Pflügers Archiv - European Journal of Physiology, Vol. 466, No. 7, 2014, p. 1227-1240.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Lopez Marques, RL, Theorin, L, Palmgren, MB & Günther-Pomorski, T 2014, 'P4-ATPases: lipid flippases in cell membranes', Pflügers Archiv - European Journal of Physiology, vol. 466, no. 7, pp. 1227-1240. https://doi.org/10.1007/s00424-013-1363-4

APA

Lopez Marques, R. L., Theorin, L., Palmgren, M. B., & Günther-Pomorski, T. (2014). P4-ATPases: lipid flippases in cell membranes. Pflügers Archiv - European Journal of Physiology, 466(7), 1227-1240. https://doi.org/10.1007/s00424-013-1363-4

Vancouver

Lopez Marques RL, Theorin L, Palmgren MB, Günther-Pomorski T. P4-ATPases: lipid flippases in cell membranes. Pflügers Archiv - European Journal of Physiology. 2014;466(7):1227-1240. https://doi.org/10.1007/s00424-013-1363-4

Author

Lopez Marques, Rosa Laura ; Theorin, Lisa ; Palmgren, Michael Broberg ; Günther-Pomorski, Thomas. / P4-ATPases : lipid flippases in cell membranes. In: Pflügers Archiv - European Journal of Physiology. 2014 ; Vol. 466, No. 7. pp. 1227-1240.

Bibtex

@article{83bc7e55d82b4ad9a0f3e87fab721836,
title = "P4-ATPases: lipid flippases in cell membranes",
abstract = "Cellular membranes, notably eukaryotic plasma membranes, are equipped with special proteins that actively translocate lipids from one leaflet to the other and thereby help generate membrane lipid asymmetry. Among these ATP-driven transporters, the P4 subfamily of P-type ATPases (P4-ATPases) comprises lipid flippases that catalyze the translocation of phospholipids from the exoplasmic to the cytosolic leaflet of cell membranes. While initially characterized as aminophospholipid translocases, recent studies of individual P4-ATPase family members from fungi, plants, and animals show that P4-ATPases differ in their substrate specificities and mediate transport of a broader range of lipid substrates, including lysophospholipids and synthetic alkylphospholipids. At the same time, the cellular processes known to be directly or indirectly affected by this class of transporters have expanded to include the regulation of membrane traffic, cytoskeletal dynamics, cell division, lipid metabolism, and lipid signaling. In this review, we will summarize the basic features of P4-ATPases and the physiological implications of their lipid transport activity in the cell.",
keywords = "CDC50 protein, Flippase, Importer, Lipid asymmetry, P-type pump, Vesicle biogenesis",
author = "{Lopez Marques}, {Rosa Laura} and Lisa Theorin and Palmgren, {Michael Broberg} and Thomas G{\"u}nther-Pomorski",
note = "OA",
year = "2014",
doi = "10.1007/s00424-013-1363-4",
language = "English",
volume = "466",
pages = "1227--1240",
journal = "Pfl{\"u}gers Archiv - European Journal of Physiology",
issn = "0031-6768",
publisher = "Springer",
number = "7",

}

RIS

TY - JOUR

T1 - P4-ATPases

T2 - lipid flippases in cell membranes

AU - Lopez Marques, Rosa Laura

AU - Theorin, Lisa

AU - Palmgren, Michael Broberg

AU - Günther-Pomorski, Thomas

N1 - OA

PY - 2014

Y1 - 2014

N2 - Cellular membranes, notably eukaryotic plasma membranes, are equipped with special proteins that actively translocate lipids from one leaflet to the other and thereby help generate membrane lipid asymmetry. Among these ATP-driven transporters, the P4 subfamily of P-type ATPases (P4-ATPases) comprises lipid flippases that catalyze the translocation of phospholipids from the exoplasmic to the cytosolic leaflet of cell membranes. While initially characterized as aminophospholipid translocases, recent studies of individual P4-ATPase family members from fungi, plants, and animals show that P4-ATPases differ in their substrate specificities and mediate transport of a broader range of lipid substrates, including lysophospholipids and synthetic alkylphospholipids. At the same time, the cellular processes known to be directly or indirectly affected by this class of transporters have expanded to include the regulation of membrane traffic, cytoskeletal dynamics, cell division, lipid metabolism, and lipid signaling. In this review, we will summarize the basic features of P4-ATPases and the physiological implications of their lipid transport activity in the cell.

AB - Cellular membranes, notably eukaryotic plasma membranes, are equipped with special proteins that actively translocate lipids from one leaflet to the other and thereby help generate membrane lipid asymmetry. Among these ATP-driven transporters, the P4 subfamily of P-type ATPases (P4-ATPases) comprises lipid flippases that catalyze the translocation of phospholipids from the exoplasmic to the cytosolic leaflet of cell membranes. While initially characterized as aminophospholipid translocases, recent studies of individual P4-ATPase family members from fungi, plants, and animals show that P4-ATPases differ in their substrate specificities and mediate transport of a broader range of lipid substrates, including lysophospholipids and synthetic alkylphospholipids. At the same time, the cellular processes known to be directly or indirectly affected by this class of transporters have expanded to include the regulation of membrane traffic, cytoskeletal dynamics, cell division, lipid metabolism, and lipid signaling. In this review, we will summarize the basic features of P4-ATPases and the physiological implications of their lipid transport activity in the cell.

KW - CDC50 protein

KW - Flippase

KW - Importer

KW - Lipid asymmetry

KW - P-type pump

KW - Vesicle biogenesis

U2 - 10.1007/s00424-013-1363-4

DO - 10.1007/s00424-013-1363-4

M3 - Journal article

C2 - 24077738

AN - SCOPUS:84904657025

VL - 466

SP - 1227

EP - 1240

JO - Pflügers Archiv - European Journal of Physiology

JF - Pflügers Archiv - European Journal of Physiology

SN - 0031-6768

IS - 7

ER -

ID: 130638694