Evidence map›Paper›PMID 28122734›Full record

ReviewAmerican journal of physiology. Cell physiology2017

Caveolins and cavins in the trafficking, maturation, and degradation of caveolae: implications for cell physiology.

Anna R Busija, Hemal H Patel, Paul A Insel

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Cell physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 118 citations in OpenAlex.

  1. Article
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  4. Review
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  9. Review
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  12. p53-miR-34a feedback in lung fibroblasts regulates antifibrotic effects of CSP7, nintedanib, and pirfenidone.American journal of physiology. Lung cellular and molecular physiology · 2025
    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. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

14 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

3 authors at 1 institution in 1 country.

Anna R BusijaDepartment of Anesthesiology, University of California, San Diego, La Jolla, California.
Hemal H PatelDepartment of Anesthesiology, University of California, San Diego, La Jolla, California.
Paul A InselDepartment of Medicine, University of California, San Diego, La Jolla, California; and inseloffice@ucsd.edu.
University of California, San Diego · US

Funding

GRADUATE TRAINING IN CELLULAR &MOLECULAR PHARMACOLOGYT32GM007752 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BROWN, JOAN HELLER, HANDEL, TRACY M · 1985 to 2023
$13.5M
Caveolae, mitochondria, and cardiac protection.R01HL091071 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PATEL, HEMAL H · 2008 to 2019
$3.8M
Aging and G-protein-regulated MMP14R21AG053568 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI INSEL, PAUL A · 2016 to 2017
$426k
Novel Therapeutics for Diabetic CardiomyopathyI01BX001963 · VA · VA SAN DIEGO HEALTHCARE SYSTEM · PI PATEL, HEMAL H · 2013 to 2025
–
BLRD VA I01 BX001963NHLBI NIH HHS R01 HL091071NIA NIH HHS R21 AG053568NIGMS NIH HHS T32 GM007752
6 · The paper itself

Abstract

Caveolins (Cavs) are ~20 kDa scaffolding proteins that assemble as oligomeric complexes in lipid raft domains to form caveolae, flask-shaped plasma membrane (PM) invaginations. Caveolae ("little caves") require lipid-lipid, protein-lipid, and protein-protein interactions that can modulate the localization, conformational stability, ligand affinity, effector specificity, and other functions of proteins that are partners of Cavs. Cavs are assembled into small oligomers in the endoplasmic reticulum (ER), transported to the Golgi for assembly with cholesterol and other oligomers, and then exported to the PM as an intact coat complex. At the PM, cavins, ~50 kDa adapter proteins, oligomerize into an outer coat complex that remodels the membrane into caveolae. The structure of caveolae protects their contents (i.e., lipids and proteins) from degradation. Cellular changes, including signal transduction effects, can destabilize caveolae and produce cavin dissociation, restructuring of Cav oligomers, ubiquitination, internalization, and degradation. In this review, we provide a perspective of the life cycle (biogenesis, degradation), composition, and physiologic roles of Cavs and caveolae and identify unanswered questions regarding the roles of Cavs and cavins in caveolae and in regulating cell physiology.

Indexed as

AnimalsCaveolaeCaveolinsCell Physiological PhenomenaHumansMembrane ProteinsModels, BiologicalProtein TransportRNA-Binding ProteinsCaveolinsMembrane ProteinsRNA-Binding Proteinscaveolaecaveolincavinlipid raft

Identifiers

PMID28122734
PMCPMC5407024
OpenAlexW2580899170

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.