Evidence map›Paper›PMID 27834731›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Model for the architecture of caveolae based on a flexible, net-like assembly of Cavin1 and Caveolin discs.

Miriam Stoeber, Pascale Schellenberger, C Alistair Siebert, Cedric Leyrat, Ari Helenius, Kay Grünewald

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026
    Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Membrane Remodeling by the Collective Action of Caveolin-1.bioRxiv : the preprint server for biology · 2025
    Article
  8. Caveolin assemblies displace one bilayer leaflet to organize and bend membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Lipid Organization by the Caveolin-1 Complex.bioRxiv : the preprint server for biology · 2024
    Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Miriam StoeberDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.
Pascale SchellenbergerDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.
C Alistair SiebertDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.
Cedric LeyratDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.
Ari HeleniusInstitute of Biochemistry, Swiss Federal Institute of Technology Zurich, 8093 Zurich, Switzerland ari.helenius@bc.biol.ethz.ch kay@strubi.ox.ac.uk.
Kay GrünewaldDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom; ari.helenius@bc.biol.ethz.ch kay@strubi.ox.ac.uk.ORCID 0000-0002-4788-2691
Centre for Human Genetics · GBÉcole Polytechnique Fédérale de Lausanne · CH

Funding

Wellcome Trust 090532/Z/09/ZWellcome Trust 090895/Z/09/ZWellcome Trust 093305/Z/10/ZWellcome Trust 107806/Z/15/Z
6 · The paper itself

Abstract

Caveolae are invaginated plasma membrane domains involved in mechanosensing, signaling, endocytosis, and membrane homeostasis. Oligomers of membrane-embedded caveolins and peripherally attached cavins form the caveolar coat whose structure has remained elusive. Here, purified Cavin1 60S complexes were analyzed structurally in solution and after liposome reconstitution by electron cryotomography. Cavin1 adopted a flexible, net-like protein mesh able to form polyhedral lattices on phosphatidylserine-containing vesicles. Mutating the two coiled-coil domains in Cavin1 revealed that they mediate distinct assembly steps during 60S complex formation. The organization of the cavin coat corresponded to a polyhedral nano-net held together by coiled-coil segments. Positive residues around the C-terminal coiled-coil domain were required for membrane binding. Purified caveolin 8S oligomers assumed disc-shaped arrangements of sizes that are consistent with the discs occupying the faces in the caveolar polyhedra. Polygonal caveolar membrane profiles were revealed in tomograms of native caveolae inside cells. We propose a model with a regular dodecahedron as structural basis for the caveolae architecture.

Indexed as

AnimalsCaveolaeCaveolin 1HEK293 CellsHeLa CellsHumansMembrane ProteinsMiceMicroscopy, Electron, TransmissionModels, BiologicalModels, MolecularMultiprotein ComplexesProtein DomainsRecombinant ProteinsRNA-Binding ProteinsSequence DeletionCAV1 protein, humanCaveolin 1CAVIN1 protein, humanCavin1 protein, mouseMembrane ProteinsMultiprotein ComplexesRecombinant ProteinsRNA-Binding Proteinscaveolaecoat assemblycoat proteinselectron cryomicroscopymembrane organization

Identifiers

PMID27834731
PMCPMC5167190
OpenAlexW2551132878

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.