Evidence map›Paper›PMID 24411252›Full record

ArticleBiophysical journal2014

Geometrical membrane curvature as an allosteric regulator of membrane protein structure and function.

Asger Tonnesen, Sune M Christensen, Vadym Tkach, Dimitrios Stamou

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 53 citations in OpenAlex.

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  9. The 2018 biomembrane curvature and remodeling roadmap.Journal of physics D: Applied physics · 2018
    Article
  10. Article
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  12. Single-molecule analysis of phospholipid scrambling by TMEM16F.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Review
  14. Artificial cell mimics as simplified models for the study of cell biology.Experimental biology and medicine (Maywood, N.J.) · 2017
    Review
  15. Article
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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

4 authors at 2 institutions in 1 country.

Asger TonnesenBionanotechnology and Nanomedicine Laboratory, Department of Chemistry, University of Copenhagen, Copenhagen, Denmark; Nano-Science Center, University of Copenhagen, Copenhagen, Denmark; Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Sune M ChristensenBionanotechnology and Nanomedicine Laboratory, Department of Chemistry, University of Copenhagen, Copenhagen, Denmark; Nano-Science Center, University of Copenhagen, Copenhagen, Denmark; Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Vadym TkachBionanotechnology and Nanomedicine Laboratory, Department of Chemistry, University of Copenhagen, Copenhagen, Denmark; Nano-Science Center, University of Copenhagen, Copenhagen, Denmark; Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark.
Dimitrios StamouBionanotechnology and Nanomedicine Laboratory, Department of Chemistry, University of Copenhagen, Copenhagen, Denmark; Nano-Science Center, University of Copenhagen, Copenhagen, Denmark; Lundbeck Foundation Center for Biomembranes in Nanomedicine, University of Copenhagen, Copenhagen, Denmark. Electronic address: stamou@nano.ku.dk.
University of Copenhagen · DKLundbeck Foundation · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transmembrane proteins are embedded in cellular membranes of varied lipid composition and geometrical curvature. Here, we studied for the first time the allosteric effect of geometrical membrane curvature on transmembrane protein structure and function. We used single-channel optical analysis of the prototypic transmembrane β-barrel α-hemolysin (α-HL) reconstituted on immobilized single small unilamellar liposomes of different diameter and therefore curvature. Our data demonstrate that physiologically abundant geometrical membrane curvatures can enforce a dramatic allosteric regulation (1000-fold inhibition) of α-HL permeability. High membrane curvatures (1/diameter ~1/40 nm(-1)) compressed the effective pore diameter of α-HL from 14.2 ± 0.8 Å to 11.4 ± 0.6 Å. This reduction in effective pore area (~40%) when combined with the area compressibility of α-HL revealed an effective membrane tension of ~50 mN/m and a curvature-imposed protein deformation energy of ~7 kBT. Such substantial energies have been shown to conformationally activate, or unfold, β-barrel and α-helical transmembrane proteins, suggesting that membrane curvature could likely regulate allosterically the structure and function of transmembrane proteins in general.

Indexed as

Allosteric RegulationAmino Acid MotifsCell Membrane PermeabilityHemolysin ProteinsModels, BiologicalStaphylococcus aureusUnilamellar LiposomesHemolysin ProteinsUnilamellar Liposomes

Identifiers

PMID24411252
PMCPMC3907227
OpenAlexW1986910511

What OpenQuestion holds

Textmetadata
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.