Evidence map›Paper›PMID 33833286›Full record

ArticleScientific reports2021

Single molecule network analysis identifies structural changes to caveolae and scaffolds due to mutation of the caveolin-1 scaffolding domain.

Timothy H Wong, Ismail M Khater, Bharat Joshi, Mona Shahsavari, Ghassan Hamarneh, Ivan R Nabi

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Caveolae mechanics in cellular functions and disease.Nature reviews. Molecular cell biology · 2026
    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. SuperResNET: Model-Free Single-Molecule Network Analysis Software Achieves Molecular Resolution of Nup96.Advanced intelligent systems (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  8. Review
  9. Review
  10. Physiological functions of caveolae in endothelium.Current opinion in physiology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. 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

6 authors at 2 institutions in 1 country.

Timothy H Wong *Life Sciences Institute, Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada.
Ismail M Khater *School of Computing Science, Simon Fraser University, Burnaby, BC, V5A 1S6, Canada.
Bharat JoshiLife Sciences Institute, Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada.
Mona ShahsavariSchool of Computing Science, Simon Fraser University, Burnaby, BC, V5A 1S6, Canada.
Ghassan Hamarneh *School of Computing Science, Simon Fraser University, Burnaby, BC, V5A 1S6, Canada. hamarneh@sfu.ca.
Ivan R Nabi *Life Sciences Institute, Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada. irnabi@mail.ubc.ca.
Simon Fraser University · CAUniversity of British Columbia · CA

Funding

CIHR PJT-156424CIHR PJT-159845
6 · The paper itself

Abstract

Caveolin-1 (CAV1), the caveolae coat protein, also associates with non-caveolar scaffold domains. Single molecule localization microscopy (SMLM) network analysis distinguishes caveolae and three scaffold domains, hemispherical S2 scaffolds and smaller S1B and S1A scaffolds. The caveolin scaffolding domain (CSD) is a highly conserved hydrophobic region that mediates interaction of CAV1 with multiple effector molecules. F92A/V94A mutation disrupts CSD function, however the structural impact of CSD mutation on caveolae or scaffolds remains unknown. Here, SMLM network analysis quantitatively shows that expression of the CAV1 CSD F92A/V94A mutant in CRISPR/Cas CAV1 knockout MDA-MB-231 breast cancer cells reduces the size and volume and enhances the elongation of caveolae and scaffold domains, with more pronounced effects on S2 and S1B scaffolds. Convex hull analysis of the outer surface of the CAV1 point clouds confirms the size reduction of CSD mutant CAV1 blobs and shows that CSD mutation reduces volume variation amongst S2 and S1B CAV1 blobs at increasing shrink values, that may reflect retraction of the CAV1 N-terminus towards the membrane, potentially preventing accessibility of the CSD. Detection of point mutation-induced changes to CAV1 domains highlights the utility of SMLM network analysis for mesoscale structural analysis of oligomers in their native environment.

Indexed as

Caveolin 1Cell LineHumansMutationProtein ConformationProtein DomainsCAV1 protein, humanCaveolin 1

Identifiers

PMID33833286
PMCPMC8032680
OpenAlexW3151434734

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.