ATP11C mutation is responsible for the defect in phosphatidylserine uptake in UPS-1 cells

Takada, Naoto; Takatsu, Hiroyuki; Miyano, Rie; Nakayama, Kazuhisa; Shin, Hye‐Won

doi:10.1194/jlr.m062547

Cited by 19 publications

(20 citation statements)

References 29 publications

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“…Using UPS-1 cells defective in PtdSer translocation, the related plasma membrane-localized P4-ATPase ATP8B1 has been suggested to promote flipping of PtdSer [96]. The defect in the nonendocytic uptake of NBD-PS in these UPS-1 defective cells has now been attributed to a mutation in the ATP11C gene [97]. In contrast, in Caco-2 cells, depletion of ATP8B1 by RNAi did not lead to any PtdSer transport inhibition [98].…”

Section: P4-atpases and Cdc50 Proteins Key Regulators Of Phospholipimentioning

confidence: 95%

On the molecular mechanism of flippase- and scramblase-mediated phospholipid transport

Montigny¹,

Lyons²,

Champeil³

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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Section: P4-atpases and Cdc50 Proteins Key Regulators Of Phospholipimentioning

confidence: 95%

On the molecular mechanism of flippase- and scramblase-mediated phospholipid transport

Montigny¹,

Lyons²,

Champeil³

et al. 2016

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

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“…During apoptosis, ATP11C undergoes caspase-mediated cleavage and is consequently inactivated, thereby contributing to PS exposure on the cell surface [106, 107]. ATP11C is crucial for PS flipping in CHO-K1 cells and a lack of the functional ATP11C protein is responsible for the defect in PS uptake in UPS-1 cells [108]. …”

Section: Control Of Transbilayer Lipid Asymmetry By Atp-driven Lipmentioning

confidence: 99%

Lipid somersaults: Uncovering the mechanisms of protein-mediated lipid flipping

Pomorski

Menon

2016

Progress in Lipid Research

146

141

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Membrane lipids diffuse rapidly in the plane of the membrane but their ability to flip spontaneously across a membrane bilayer is hampered by a significant energy barrier. Thus spontaneous flip-flop of polar lipids across membranes is very slow, even though it must occur rapidly to support diverse aspects of cellular life. Here we discuss the mechanisms by which rapid flip-flop occurs, and what role lipid flipping plays in membrane homeostasis and cell growth. We focus on conceptual aspects, highlighting mechanistic insights from biochemical and in silico experiments, and the recent, ground-breaking identification of a number of lipid scramblases.

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“…Previously, we demonstrated that ATP10A and ATP8B1 preferentially translocate NBD‐labeled PC (NBD‐PC), and ATP11A and ATP11C specifically translocate NBD‐PS and NBD‐PE from the outer/exoplasmic to inner/cytoplasmic leaflet of the plasma membrane . The NBD‐PC‐flippase activity of ATP10A is higher than that of ATP8B1 , and ATP11C prefers NBD‐PS to NBD‐PE .…”

Section: Resultsmentioning

confidence: 99%

“…Previously, we demonstrated that ATP10A and ATP8B1 preferentially translocate NBD-labeled PC (NBD-PC), and ATP11A and ATP11C specifically translocate NBD-PS and NBD-PE from the outer/exoplasmic to inner/cytoplasmic leaflet of the plasma membrane [25][26][27]. The NBD-PC-flippase activity of ATP10A is higher than that of ATP8B1 [26], and ATP11C prefers NBD-PS to NBD-PE [25,27]. We also showed that cell adhesion was delayed in cells stably expressing ATP10A but not its ATPase-deficient mutant, ATP10A(E203Q) [26].…”

Section: Resultsmentioning

confidence: 99%

Alteration of transbilayer phospholipid compositions is involved in cell adhesion, cell spreading, and focal adhesion formation

et al. 2016

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We previously showed that P4-ATPases, ATP10A/ATP8B1, and ATP11A/ ATP11C have flippase activities toward phosphatidylcholine (PC), and aminophospholipids [phosphatidylserine (PS) and phosphatidylethanolamine], respectively. Here, we investigate the effect of PC-specific flippases versus aminophospholipid-specific flippases in cell spreading on the extracellular matrix. Expression of PC-flippases, but not PS-flippases, delayed cell adhesion, cell spreading and inhibited formation of focal adhesions. In addition, overexpression of a PS-binding probe that sequesters PS in the cytoplasmic leaflet delayed cell spreading and inhibited formation of focal adhesions. These results suggest that elevation of PC at the cytoplasmic leaflet of the plasma membrane by expression of PC-flippases may reduce the local concentration of PS or phosphoinositides, required for efficient cell adhesion, focal adhesion formation, and cell spreading.

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ATP11C mutation is responsible for the defect in phosphatidylserine uptake in UPS-1 cells

Cited by 19 publications

References 29 publications

On the molecular mechanism of flippase- and scramblase-mediated phospholipid transport

On the molecular mechanism of flippase- and scramblase-mediated phospholipid transport

Lipid somersaults: Uncovering the mechanisms of protein-mediated lipid flipping

Alteration of transbilayer phospholipid compositions is involved in cell adhesion, cell spreading, and focal adhesion formation

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