Evidence map›Paper›PMID 32049332›Full record

ReviewBiochemical Society transactions2020

Keeping in touch with the membrane; protein- and lipid-mediated confinement of caveolae to the cell surface.

Madlen Hubert, Elin Larsson, Richard Lundmark

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Membrane Remodeling by the Collective Action of Caveolin-1.bioRxiv : the preprint server for biology · 2025
    Article
  7. 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
  8. Article
  9. Review
  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. Cells · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Membrane insertion mechanism of the caveola coat protein Cavin1.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article
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

3 authors at 1 institution in 1 country.

Madlen HubertDepartment of Integrative Medical Biology, Umeå University, Umeå SE-901 87, Sweden.
Elin LarssonDepartment of Integrative Medical Biology, Umeå University, Umeå SE-901 87, Sweden.
Richard LundmarkDepartment of Integrative Medical Biology, Umeå University, Umeå SE-901 87, Sweden.
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Caveolae are small Ω-shaped invaginations of the plasma membrane that play important roles in mechanosensing, lipid homeostasis and signaling. Their typical morphology is characterized by a membrane funnel connecting a spherical bulb to the membrane. Membrane funnels (commonly known as necks and pores) are frequently observed as transient states during fusion and fission of membrane vesicles in cells. However, caveolae display atypical dynamics where the membrane funnel can be stabilized over an extended period of time, resulting in cell surface constrained caveolae. In addition, caveolae are also known to undergo flattening as well as short-range cycles of fission and fusion with the membrane, requiring that the membrane funnel closes or opens up, respectively. This mini-review considers the transition between these different states and highlights the role of the protein and lipid components that have been identified to control the balance between surface association and release of caveolae.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCaveolaeCaveolin 1FilaminsHeLa CellsHumansMembrane LipidsMiceMice, KnockoutSignal TransductionAdaptor Proteins, Signal TransducingCarrier ProteinsCaveolin 1EHD2 protein, mouseFilaminsMembrane LipidsPACSIN2 protein, humancaveolaecaveolincholesteroldynamicsEHD2pacsin2

Identifiers

PMID32049332
PMCPMC7054752
OpenAlexW3005585198

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.