Evidence map›Paper›PMID 32719316›Full record

ArticleScientific reports2020

An optogenetic system to control membrane phospholipid asymmetry through flippase activation in budding yeast.

Tomomi Suzuki, Tetsuo Mioka, Kazuma Tanaka, Akira Nagatani

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Synthetic Lipid Biology.Chemical reviews · 2025
    Review
  2. Review
  3. Review
  4. Expanding horizons of biosciences by light-control.Biophysics and physicobiology · 2021
    Article
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

4 authors at 2 institutions in 1 country.

Tomomi SuzukiDepartment of Botany, Graduate School of Science, Kyoto University, Oiwake-cho, Kitashirakawa, Sakyo-ku, Kyoto, 606-8502, Japan. tomo@physiol.bot.kyoto-u.ac.jp.
Tetsuo MiokaDivision of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Life Science, Kita-ku, Sapporo, 060-0815, Japan.
Kazuma TanakaDivision of Molecular Interaction, Institute for Genetic Medicine, Hokkaido University Graduate School of Life Science, Kita-ku, Sapporo, 060-0815, Japan.
Akira NagataniDepartment of Botany, Graduate School of Science, Kyoto University, Oiwake-cho, Kitashirakawa, Sakyo-ku, Kyoto, 606-8502, Japan. nagatani@physiol.bot.kyoto-u.ac.jp.
Hokkaido University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipid asymmetry in biological membranes is essential for various cell functions, such as cell polarity, cytokinesis, and apoptosis. P4-ATPases (flippases) are involved in the generation of such asymmetry. In Saccharomyces cerevisiae, the protein kinases Fpk1p/Fpk2p activate the P4-ATPases Dnf1p/Dnf2p by phosphorylation. Previously, we have shown that a blue-light-dependent protein kinase, phototropin from Chlamydomonas reinhardtii (CrPHOT), complements defects in an fpk1Δ fpk2Δ mutant. Herein, we investigated whether CrPHOT optically regulates P4-ATPase activity. First, we demonstrated that the translocation of NBD-labelled phospholipids to the cytoplasmic leaflet via P4-ATPases was promoted by blue-light irradiation in fpk1Δ fpk2Δ cells with CrPHOT. In addition, blue light completely suppressed the defects in membrane functions (such as endocytic recycling, actin depolarization, and apical-isotropic growth switching) caused by fpk1Δ fpk2Δ mutations. All responses required the kinase activity of CrPHOT. Hence, these results indicate the utility of CrPHOT as a powerful and first tool for optogenetic manipulation of P4-ATPase activity.

Indexed as

Adenosine TriphosphatasesATP-Binding Cassette TransportersCell MembraneEnzyme ActivationOptogeneticsPhospholipidsPhosphorylationProtein KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesATP-Binding Cassette TransportersDnf1 protein, S cerevisiaeDnf2 protein, S cerevisiaeFpk1 protein, S cerevisiaeFpk2 protein, S cerevisiaePhospholipidsProtein KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID32719316
PMCPMC7385178
OpenAlexW3044820835

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.