Evidence map›Paper›PMID 33568658›Full record

ArticleNature communications2021

Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation.

Vikas A Tillu, James Rae, Ya Gao, Nicholas Ariotti, Matthias Floetenmeyer, Oleksiy Kovtun, Kerrie-Ann McMahon, Natasha Chaudhary, Robert G Parton, Brett M Collins

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Extracellular Mitochondria Mediate Endothelial Injury After Traumatic Brain Injury.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Article
  3. Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Membrane Remodeling by the Collective Action of Caveolin-1.bioRxiv : the preprint server for biology · 2025
    Article
  11. Review
  12. Article
  13. 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
  14. Review
  15. Article
  16. Article
  17. Caveolae: Metabolic Platforms at the Crossroads of Health and Disease.International journal of molecular sciences · 2025
    Review
  18. Review
  19. Article
  20. Review
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

10 authors at 4 institutions in 4 countries.

Vikas A TilluInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia.ORCID http://orcid.org/0000-0002-1034-9543
James RaeInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia.
Ya GaoInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia.ORCID http://orcid.org/0000-0001-9327-5051
Nicholas AriottiElectron Microscope Unit, The University of New South Wales, Kensington, NSW, Australia.
Matthias FloetenmeyerCentre for Microscopy and Microanalysis, St. Lucia, QLD, Australia.
Oleksiy KovtunInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia.ORCID http://orcid.org/0000-0001-6374-7863
Kerrie-Ann McMahonInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia.
Natasha ChaudharyInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia.
Robert G PartonInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia. r.parton@imb.uq.edu.au.ORCID http://orcid.org/0000-0002-7494-5248
Brett M CollinsInstitute for Molecular Bioscience, The University of Queensland, St. Lucia, QLD, Australia. b.collins@imb.uq.edu.au.ORCID http://orcid.org/0000-0002-6070-3774
The University of Queensland · AUCentre for Microscopy and Microanalysis · AUMount Sinai Hospital · CAUNSW Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Caveolae are spherically shaped nanodomains of the plasma membrane, generated by cooperative assembly of caveolin and cavin proteins. Cavins are cytosolic peripheral membrane proteins with negatively charged intrinsically disordered regions that flank positively charged α-helical regions. Here, we show that the three disordered domains of Cavin1 are essential for caveola formation and dynamic trafficking of caveolae. Electrostatic interactions between disordered regions and α-helical regions promote liquid-liquid phase separation behaviour of Cavin1 in vitro, assembly of Cavin1 oligomers in solution, generation of membrane curvature, association with caveolin-1, and Cavin1 recruitment to caveolae in cells. Removal of the first disordered region causes irreversible gel formation in vitro and results in aberrant caveola trafficking through the endosomal system. We propose a model for caveola assembly whereby fuzzy electrostatic interactions between Cavin1 and caveolin-1 proteins, combined with membrane lipid interactions, are required to generate membrane curvature and a metastable caveola coat.

Indexed as

Amino Acid SequenceAnimalsCaveolaeCaveolin 1Cell MembraneMembrane ProteinsMiceProtein DomainsRNA-Binding ProteinsStatic ElectricityCaveolin 1Cavin1 protein, mouseMembrane ProteinsRNA-Binding Proteins

Identifiers

PMID33568658
PMCPMC7875971
OpenAlexW3127128904

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.