Evidence map›Paper›PMID 32029718›Full record

ArticleNature communications2020

Regulation of lipid saturation without sensing membrane fluidity.

Stephanie Ballweg, Erdinc Sezgin, Milka Doktorova, Roberto Covino, John Reinhard, Dorith Wunnicke, Inga Hänelt, Ilya Levental, Gerhard Hummer, Robert Ernst

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

105 citing papers in PubMed, 187 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Adaptive responses ofBiotechnology reports (Amsterdam, Netherlands) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Roles of FXR in Lipid Biochemistry within Hepatocellular Carcinoma Using MALDI MSI.Journal of the American Society for Mass Spectrometry · 2026
    Article
  11. Article
  12. Article
  13. Optimizing mRNA delivery with targeted elastin-like polypeptide-based LENN formulations: Insights into the endocytosis mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

45 more citing papers are in PubMed but not listed here.

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

10 authors at 5 institutions in 3 countries.

Stephanie BallwegMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Kirrberger Strasse 100, Building 61.4, 66421, Homburg, Germany.
Erdinc SezginMRC Human Immunology Unit, MRC Weatherall Institute of Molecular Medicine, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0002-4915-388X
Milka DoktorovaDepartment of Integrative Biology and Pharmacology, McGovern Medical School at the University of Texas Health Science Center, Houston, Texas, USA.
Roberto CovinoDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438, Frankfurt, Germany.ORCID http://orcid.org/0000-0003-0884-0402
John ReinhardMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Kirrberger Strasse 100, Building 61.4, 66421, Homburg, Germany.
Dorith WunnickeInstitute of Biochemistry, Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438, Frankfurt, Germany.
Inga HäneltInstitute of Biochemistry, Goethe University Frankfurt, Max-von-Laue-Strasse 9, 60438, Frankfurt, Germany.ORCID http://orcid.org/0000-0003-1495-3163
Ilya LeventalDepartment of Integrative Biology and Pharmacology, McGovern Medical School at the University of Texas Health Science Center, Houston, Texas, USA.ORCID http://orcid.org/0000-0002-1206-9545
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-7768-746X
Robert ErnstMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Kirrberger Strasse 100, Building 61.4, 66421, Homburg, Germany. robert.ernst@uks.eu.ORCID http://orcid.org/0000-0002-0283-3490
Goethe University Frankfurt · DESaarland University · DEThe University of Texas Health Science Center at Houston · USMax Planck Institute of Biophysics · DEUniversity of Oxford · GB

Funding

Lipidomic, biophysical, and functional differentiation of Mesenchymal Stem Cell membranesR01GM114282 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI LEVENTAL, ILYA · 2015 to 2019
$1.7M
Effects of lipidomic diversity on GPCRR01GM120351 · NIGMS · UNIVERSITY OF DELAWARE · PI LYMAN, EDWARD RAY · 2017 to 2021
$1.6M
Structural determinants and functional consequences of protein partitioning to ordered membrane microdomains.R01GM124072 · NIGMS · UNIVERSITY OF VIRGINIA · PI LEVENTAL, ILYA · 2017 to 2019
$961k
NIGMS NIH HHS R01 GM114282NIGMS NIH HHS R01 GM120351NIGMS NIH HHS R01 GM124072
6 · The paper itself

Abstract

Cells maintain membrane fluidity by regulating lipid saturation, but the molecular mechanisms of this homeoviscous adaptation remain poorly understood. We have reconstituted the core machinery for regulating lipid saturation in baker's yeast to study its molecular mechanism. By combining molecular dynamics simulations with experiments, we uncover a remarkable sensitivity of the transcriptional regulator Mga2 to the abundance, position, and configuration of double bonds in lipid acyl chains, and provide insights into the molecular rules of membrane adaptation. Our data challenge the prevailing hypothesis that membrane fluidity serves as the measured variable for regulating lipid saturation. Rather, we show that Mga2 senses the molecular lipid-packing density in a defined region of the membrane. Our findings suggest that membrane property sensors have evolved remarkable sensitivities to highly specific aspects of membrane structure and dynamics, thus paving the way toward the development of genetically encoded reporters for such properties in the future.

Indexed as

Amino Acid SubstitutionBiosensing TechniquesFluorescence Resonance Energy TransferMembrane FluidityMembrane LipidsMembrane ProteinsModels, BiologicalMolecular Dynamics SimulationMutagenesis, Site-DirectedSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsMembrane LipidsMembrane ProteinsMGA2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID32029718
PMCPMC7005026
OpenAlexW3004520297

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.