Evidence map›Paper›PMID 24473072›Full record

ArticleeLife2013

Single-molecule analysis reveals self assembly and nanoscale segregation of two distinct cavin subcomplexes on caveolae.

Yann Gambin, Nicholas Ariotti, Kerrie-Ann McMahon, Michele Bastiani, Emma Sierecki, Oleksiy Kovtun, Mark E Polinkovsky, Astrid Magenau, Wooram Jung, Satomi Okano and 9 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
8.5field-weighted citation impact, top 1% 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

68 citing papers in PubMed, 138 citations in OpenAlex.

  1. Review
  2. Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. The Role of Membrane Lipids in the Formation and Function of Caveolae.Cold Spring Harbor perspectives in biology · 2023
    Review
  13. Review
  14. Article
  15. Membrane insertion mechanism of the caveola coat protein Cavin1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

8 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

19 authors at 2 institutions in 1 country.

Yann GambinInstitute for Molecular Bioscience, The University of Queensland, Brisbane, Australia.
Nicholas Ariotti
Kerrie-Ann McMahon
Michele Bastiani
Emma Sierecki
Oleksiy Kovtun
Mark E Polinkovsky
Astrid Magenau
Wooram Jung
Satomi Okano
Yong Zhou
Natalya Leneva
Sergey Mureev
Wayne Johnston
Katharina Gaus
John F Hancock
Brett M Collins
Kirill Alexandrov
Robert G Parton
University of Queensland · AUUNSW Sydney · AU

Funding

Structure and Function of Plasma membrane NanodomainsR01GM066717 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI HANCOCK, JOHN F · 2003 to 2012
$2.4M
6 · The paper itself

Abstract

In mammalian cells three closely related cavin proteins cooperate with the scaffolding protein caveolin to form membrane invaginations known as caveolae. Here we have developed a novel single-molecule fluorescence approach to directly observe interactions and stoichiometries in protein complexes from cell extracts and from in vitro synthesized components. We show that up to 50 cavins associate on a caveola. However, rather than forming a single coat complex containing the three cavin family members, single-molecule analysis reveals an exquisite specificity of interactions between cavin1, cavin2 and cavin3. Changes in membrane tension can flatten the caveolae, causing the release of the cavin coat and its disassembly into separate cavin1-cavin2 and cavin1-cavin3 subcomplexes. Each of these subcomplexes contain 9 ± 2 cavin molecules and appear to be the building blocks of the caveolar coat. High resolution immunoelectron microscopy suggests a remarkable nanoscale organization of these separate subcomplexes, forming individual striations on the surface of caveolae. DOI: http://dx.doi.org/10.7554/eLife.01434.001.

Indexed as

Protein MultimerizationAnimalsCarrier ProteinsCaveolaeCell LineIntracellular Signaling Peptides and ProteinsMicroscopy, ImmunoelectronMolecular ImagingOptical ImagingPhosphate-Binding ProteinsProtein BindingRNA-Binding ProteinsCarrier ProteinsCAVIN1 protein, humanCAVIN2 protein, humanCAVIN3 protein, humanIntracellular Signaling Peptides and ProteinsPhosphate-Binding ProteinsRNA-Binding Proteinscaveolaecell-free protein expressionsingle-molecule

Identifiers

PMID24473072
PMCPMC3903133
OpenAlexW2126743037

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.