Evidence map›Paper›PMID 36729022›Full record

ArticleThe Journal of cell biology2023

Dynamin2 functions as an accessory protein to reduce the rate of caveola internalization.

Elin Larsson, Björn Morén, Kerrie-Ann McMahon, Robert G Parton, Richard Lundmark

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.8field-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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Caveolae: Metabolic Platforms at the Crossroads of Health and Disease.International journal of molecular sciences · 2025
    Review
  10. Article
  11. Is endocytosis by caveolae dependent on dynamin?Nature reviews. Molecular cell biology · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. The Role of Membrane Lipids in the Formation and Function of Caveolae.Cold Spring Harbor perspectives in biology · 2023
    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

5 authors at 2 institutions in 2 countries.

Elin LarssonIntegrative Medical Biology, Umeå University , Umeå, Sweden.ORCID 0000-0003-4224-8226
Björn MorénIntegrative Medical Biology, Umeå University , Umeå, Sweden.ORCID 0000-0002-4252-6903
Kerrie-Ann McMahonInstitute for Molecular Bioscience, The University of Queensland , Brisbane, Queensland, Australia.ORCID 0000-0002-0833-5708
Robert G PartonInstitute for Molecular Bioscience, The University of Queensland , Brisbane, Queensland, Australia.ORCID 0000-0002-7494-5248
Richard LundmarkIntegrative Medical Biology, Umeå University , Umeå, Sweden.ORCID 0000-0001-9104-724X
Umeå University · SEThe University of Queensland · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Caveolae are small membrane invaginations that generally are stably attached to the plasma membrane. Their release is believed to depend on the GTPase dynamin 2 (Dyn2), in analogy with its role in fission of clathrin-coated vesicles. The mechanistic understanding of caveola fission is, however, sparse. Here, we used microscopy-based tracking of individual caveolae in living cells to determine the role of Dyn2 in caveola dynamics. We report that Dyn2 stably associated with the bulb of a subset of caveolae, but was not required for formation or fission of caveolae. Dyn2-positive caveolae displayed longer plasma membrane duration times, whereas depletion of Dyn2 resulted in shorter duration times and increased caveola fission. The stabilizing role of Dyn2 was independent of its GTPase activity and the caveola stabilizing protein EHD2. Thus, we propose that, in contrast to the current view, Dyn2 is not a core component of the caveolae machinery, but rather functions as an accessory protein that restrains caveola internalization.

Indexed as

CaveolaeDynamin IIEndocytosisGTP PhosphohydrolasesDynamin IIGTP Phosphohydrolases

Identifiers

PMID36729022
PMCPMC9929934
OpenAlexW4318924397

What Socratic 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 Socratic graph.