Evidence map›Paper›PMID 34038161›Full record

ArticleMolecular biology of the cell2021

Phospholipid flippases and Sfk1 are essential for the retention of ergosterol in the plasma membrane.

Takuma Kishimoto, Tetsuo Mioka, Eriko Itoh, David E Williams, Raymond J Andersen, Kazuma Tanaka

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 33 citations in OpenAlex.

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  8. Secondary Metabolites Produced by the Blue-Cheese Ripening MoldJournal of fungi (Basel, Switzerland) · 2023
    Review
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  14. Review
  15. A Role of Phosphatidylserine in the Function of Recycling Endosomes.Frontiers in cell and developmental biology · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Takuma KishimotoDivision of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Life Science, Sapporo, Hokkaido 060-0815, Japan.
Tetsuo MiokaDivision of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Life Science, Sapporo, Hokkaido 060-0815, Japan.
Eriko ItohDivision of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Life Science, Sapporo, Hokkaido 060-0815, Japan.
David E WilliamsDepartments of Chemistry and Earth, Ocean, and Atmospheric Sciences, University of British Columbia, Vancouver, BC V6T 1Z1, Canada.
Raymond J AndersenDepartments of Chemistry and Earth, Ocean, and Atmospheric Sciences, University of British Columbia, Vancouver, BC V6T 1Z1, Canada.
Kazuma TanakaDivision of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Life Science, Sapporo, Hokkaido 060-0815, Japan.
Hokkaido University · JPUniversity of British Columbia · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sterols are important lipid components of the plasma membrane (PM) in eukaryotic cells, but it is unknown how the PM retains sterols at a high concentration. Phospholipids are asymmetrically distributed in the PM, and phospholipid flippases play an important role in generating this phospholipid asymmetry. Here, we provide evidence that phospholipid flippases are essential for retaining ergosterol in the PM of yeast. A mutant in three flippases, Dnf1-Lem3, Dnf2-Lem3, and Dnf3-Crf1, and a membrane protein, Sfk1, showed a severe growth defect. We recently identified Sfk1 as a PM protein involved in phospholipid asymmetry. The PM of this mutant showed high permeability and low density. Staining with the sterol probe filipin and the expression of a sterol biosensor revealed that ergosterol was not retained in the PM. Instead, ergosterol accumulated in an esterified form in lipid droplets. We propose that ergosterol is retained in the PM by the asymmetrical distribution of phospholipids and the action of Sfk1. Once phospholipid asymmetry is severely disrupted, sterols might be exposed on the cytoplasmic leaflet of the PM and actively transported to the endoplasmic reticulum by sterol transfer proteins.

Indexed as

Adenosine TriphosphatasesATP-Binding Cassette TransportersCell MembraneErgosterolMembrane ProteinsMembrane Transport ProteinsPhospholipid Transfer ProteinsRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesATP-Binding Cassette TransportersCRF1 protein, S cerevisiaeDnf1 protein, S cerevisiaeDnf2 protein, S cerevisiaeDnf3 protein, S cerevisiaeErgosterolLem3 protein, S cerevisiaeMembrane ProteinsMembrane Transport ProteinsPhospholipid Transfer ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSfk1 protein, S cerevisiae

Identifiers

PMID34038161
PMCPMC8694040
OpenAlexW3164411947

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.