Evidence map›Paper›PMID 31601944›Full record

ArticleScientific reports2019

Curvature induction and sensing of the F-BAR protein Pacsin1 on lipid membranes via molecular dynamics simulations.

Md Iqbal Mahmood, Hiroshi Noguchi, Kei-Ichi Okazaki

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Bridging Scales: Coarse-Grained Protein Models in Computational Biology.Advances in experimental medicine and biology · 2026
    Review
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  5. Review
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  7. Unveiling Interactions between Self-Assembling Peptides and Neuronal Membranes.Langmuir : the ACS journal of surfaces and colloids · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Molecular Dynamics Simulations of Curved Lipid Membranes.International journal of molecular sciences · 2022
    Review
  14. Review
  15. Article
  16. Membrane signalosome: where biophysics meets systems biology.Current opinion in systems biology · 2021
    Article
  17. Article
  18. Mechanisms of negative membrane curvature sensing and generation by ESCRT III subunit Snf7.Protein science : a publication of the Protein Society · 2020
    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

3 authors at 2 institutions in 1 country.

Md Iqbal MahmoodDepartment of Theoretical and Computational Molecular Science, Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, 444-8585, Japan.
Hiroshi NoguchiInstitute for Solid State Physics, University of Tokyo, Kashiwa, Chiba, 277-8581, Japan.ORCID http://orcid.org/0000-0003-1735-7586
Kei-Ichi OkazakiDepartment of Theoretical and Computational Molecular Science, Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, 444-8585, Japan. keokazaki@ims.ac.jp.ORCID http://orcid.org/0000-0003-2168-3069
National Institutes of Natural Sciences · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

F-Bin/Amphiphysin/Rvs (F-BAR) domain proteins play essential roles in biological processes that involve membrane remodelling, such as endocytosis and exocytosis. It has been shown that such proteins transform the lipid membrane into tubes. Notably, Pacsin1 from the Pacsin/Syndapin subfamily has the ability to transform the membrane into various morphologies: striated tubes, featureless wide and thin tubes, and pearling vesicles. The molecular mechanism of this interesting ability remains elusive. In this study, we performed all-atom (AA) and coarse-grained (CG) molecular dynamics simulations to investigate the curvature induction and sensing mechanisms of Pacsin1 on a membrane. From AA simulations, we show that Pacsin1 has internal structural flexibility. In CG simulations with parameters tuned from the AA simulations, spontaneous assembly of two Pacsin1 dimers through lateral interaction is observed. Based on the complex structure, we show that the regularly assembled Pacsin1 dimers bend a tensionless membrane. We also show that a single Pacsin1 dimer senses the membrane curvature, binding to a buckled membrane with a preferred curvature. These results provide molecular insights into polymorphic membrane remodelling.

Indexed as

Adaptor Proteins, Signal TransducingCell MembraneComputer SimulationCrystallography, X-RayEndocytosisHumansMembrane LipidsMolecular Dynamics SimulationNerve Tissue ProteinsProtein MultimerizationProtein Structure, TertiaryAdaptor Proteins, Signal TransducingamphiphysinMembrane LipidsNerve Tissue ProteinsPACSIN1 protein, human

Identifiers

PMID31601944
PMCPMC6787258
OpenAlexW2979465241

What Socratic holds

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LicenceCC BY
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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 Socratic graph.