Evidence map›Paper›PMID 29941475›Full record

ArticleThe Journal of cell biology2018

The molecular recognition of phosphatidic acid by an amphipathic helix in Opi1.

Harald F Hofbauer, Michael Gecht, Sabine C Fischer, Anja Seybert, Achilleas S Frangakis, Ernst H K Stelzer, Roberto Covino, Gerhard Hummer, Robert Ernst

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
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  4. Nir2 crystal structures reveal a phosphatidic acid-sensing mechanism at ER-PM contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Exploring lipid-protein interactions in plant membranes.Journal of experimental botany · 2024
    Review
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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

9 authors at 3 institutions in 1 country.

Harald F HofbauerBuchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany harald.f.hofbauer@gmail.com.ORCID 0000-0003-2617-5901
Michael GechtBuchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany.ORCID 0000-0002-4643-6593
Sabine C FischerBuchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany.
Anja SeybertBuchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany.
Achilleas S FrangakisBuchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany.
Ernst H K StelzerBuchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt, Germany.
Roberto CovinoDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Frankfurt, Germany.
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID 0000-0001-7768-746X
Robert ErnstInstitute of Medical Biochemistry and Molecular Biology, School of Medicine, University of Saarland, Homburg, Germany robert.ernst@uks.eu.ORCID 0000-0002-0283-3490
Goethe University Frankfurt · DEMax Planck Institute of Biophysics · DESaarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A key event in cellular physiology is the decision between membrane biogenesis and fat storage. Phosphatidic acid (PA) is an important intermediate at the branch point of these pathways and is continuously monitored by the transcriptional repressor Opi1 to orchestrate lipid metabolism. In this study, we report on the mechanism of membrane recognition by Opi1 and identify an amphipathic helix (AH) for selective binding of PA over phosphatidylserine (PS). The insertion of the AH into the membrane core renders Opi1 sensitive to the lipid acyl chain composition and provides a means to adjust membrane biogenesis. By rational design of the AH, we tune the membrane-binding properties of Opi1 and control its responsiveness in vivo. Using extensive molecular dynamics simulations, we identify two PA-selective three-finger grips that tightly bind the PA phosphate headgroup while interacting less intimately with PS. This work establishes lipid headgroup selectivity as a new feature in the family of AH-containing membrane property sensors.

Indexed as

Binding SitesGene Expression Regulation, FungalHydrophobic and Hydrophilic InteractionsLipid MetabolismMolecular Dynamics SimulationPhosphatidic AcidsPhosphatidylserinesProtein BindingRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionOPI1 protein, S cerevisiaePhosphatidic AcidsPhosphatidylserinesRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID29941475
PMCPMC6122994
OpenAlexW2788277007

What OpenQuestion holds

Textmetadata
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.