Evidence map›Paper›PMID 23740253›Full record

ArticleThe Journal of biological chemistry2013

α-Synuclein senses lipid packing defects and induces lateral expansion of lipids leading to membrane remodeling.

Myriam M Ouberai, Juan Wang, Marcus J Swann, Celine Galvagnion, Tim Guilliams, Christopher M Dobson, Mark E Welland

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

106 citing papers in PubMed, 205 citations in OpenAlex.

  1. Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. The disordered and structured regions ofbioRxiv : the preprint server for biology · 2026
    Article
  6. Article
  7. Lipid-packing defects are sufficient to modulate membrane insertion and the bound state of α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Parkinson disease is a fatty acidopathy.Nature reviews. Neurology · 2025
    Review
  9. Dysregulation of Monounsaturated Fatty Acids is Related to α-Synuclein in Multiple System Atrophy.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
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  19. Article
  20. α-Synuclein and biological membranes: the danger of loving too much.Chemical communications (Cambridge, England) · 2023
    Review

46 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

7 authors at 2 institutions in 1 country.

Myriam M OuberaiFrom the Nanoscience Centre, Department of Engineering, University of Cambridge, Cambridge CB3 0FF, United Kingdom,. Electronic address: mmo25@cam.ac.uk.
Juan Wangthe Farfield Group Ltd., Biolin Scientific, Voyager, Chicago Avenue, Manchester M90 3DQ, United Kingdom, and.
Marcus J Swannthe Farfield Group Ltd., Biolin Scientific, Voyager, Chicago Avenue, Manchester M90 3DQ, United Kingdom, and.
Celine Galvagnionthe Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
Tim Guilliamsthe Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
Christopher M Dobsonthe Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
Mark E WellandFrom the Nanoscience Centre, Department of Engineering, University of Cambridge, Cambridge CB3 0FF, United Kingdom.
University of Cambridge · GBBiolin Scientific (United Kingdom) · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H003843/1Parkinson's UK H-0903
6 · The paper itself

Abstract

There is increasing evidence for the involvement of lipid membranes in both the functional and pathological properties of α-synuclein (α-Syn). Despite many investigations to characterize the binding of α-Syn to membranes, there is still a lack of understanding of the binding mode linking the properties of lipid membranes to α-Syn insertion into these dynamic structures. Using a combination of an optical biosensing technique and in situ atomic force microscopy, we show that the binding strength of α-Syn is related to the specificity of the lipid environment (the lipid chemistry and steric properties within a bilayer structure) and to the ability of the membranes to accommodate and remodel upon the interaction of α-Syn with lipid membranes. We show that this interaction results in the insertion of α-Syn into the region of the headgroups, inducing a lateral expansion of lipid molecules that can progress to further bilayer remodeling, such as membrane thinning and expansion of lipids out of the membrane plane. We provide new insights into the affinity of α-Syn for lipid packing defects found in vesicles of high curvature and in planar membranes with cone-shaped lipids and suggest a comprehensive model of the interaction between α-Syn and lipid bilayers. The ability of α-Syn to sense lipid packing defects and to remodel membrane structure supports its proposed role in vesicle trafficking.

Indexed as

alpha-SynucleinInterferometryLipid BilayersMelittenMembrane LipidsMembrane ProteinsModels, MolecularPermeabilityPhospholipidsProtein BindingProtein Structure, SecondaryTissue ExtractsUnilamellar Liposomesalpha-SynucleinLipid BilayersMelittenMembrane LipidsMembrane ProteinsPhospholipidsTissue ExtractsUnilamellar Liposomesalpha-SynucleinAtomic Force MicroscopyDual Polarization InterferometryLipid Packing DefectsMembrane BilayerMembrane BiophysicsMembrane RemodelingMembrane StructureProtein-Lipid Interactions

Identifiers

PMID23740253
PMCPMC3774359
OpenAlexW1969091108

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.