Journal
FEBS LETTERS
Volume 589, Issue 24, Pages 3908-3914Publisher
WILEY
DOI: 10.1016/j.febslet.2015.11.031
Keywords
P-type ATPase; Flippase; Interaction site; CDC50; TMEM30; Membrane transport
Funding
- Danish Medical Research Council
- Novo Nordisk Foundation
- Lundbeck Foundation
- Canadian Institutes for Health Research [MOP-106667]
- Lundbeck Foundation [R93-2011-8682, R118-2012-11726] Funding Source: researchfish
- Novo Nordisk Fonden [NNF14OC0011639, NNF14OC0013409] Funding Source: researchfish
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P4-ATPases, or flippases, translocate phospholipids between the two leaflets of eukaryotic biological membranes. They are essential to the physiologically crucial phospholipid asymmetry and involved in severe diseases, but their molecular structure and mechanism are still unresolved. Here, we show that in an extensive mutational alanine screening of the mammalian flippase ATP8A2 catalytic subunit, five mutations stand out by leading to reduced glycosylation of the accessory subunit CDC50A. These mutations may disturb the interaction between the subunits. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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