The transport mechanism of P4 ATPase lipid flippases
(2020) In The Biochemical journal 477(19). p.3769-3790- 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... (More)
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.
(Less)
- author
- López-Marqués, Rosa L. ; Gourdon, Pontus LU ; Günther Pomorski, Thomas and Palmgren, Michael
- organization
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- autoinhibition, CDC50 protein, cryo-electron microscopy, flippases, lipid transport, P4 ATPases
- in
- The Biochemical journal
- volume
- 477
- issue
- 19
- pages
- 22 pages
- publisher
- Portland Press
- external identifiers
-
- scopus:85092886707
- pmid:33045059
- ISSN
- 0264-6021
- DOI
- 10.1042/BCJ20200249
- language
- English
- LU publication?
- yes
- id
- ca3b07bb-2f1f-4d5a-b3e1-03f8d6fcf759
- date added to LUP
- 2020-11-06 09:06:03
- date last changed
- 2024-06-12 23:52:09
@article{ca3b07bb-2f1f-4d5a-b3e1-03f8d6fcf759,
abstract = {{<p>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.</p>}},
author = {{López-Marqués, Rosa L. and Gourdon, Pontus and Günther Pomorski, Thomas and Palmgren, Michael}},
issn = {{0264-6021}},
keywords = {{autoinhibition; CDC50 protein; cryo-electron microscopy; flippases; lipid transport; P4 ATPases}},
language = {{eng}},
number = {{19}},
pages = {{3769--3790}},
publisher = {{Portland Press}},
series = {{The Biochemical journal}},
title = {{The transport mechanism of P4 ATPase lipid flippases}},
url = {{http://dx.doi.org/10.1042/BCJ20200249}},
doi = {{10.1042/BCJ20200249}},
volume = {{477}},
year = {{2020}},
}