ArticleScientific reports2019
Super-resolution modularity analysis shows polyhedral caveolin-1 oligomers combine to form scaffolds and caveolae.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Membrane remodeling by the collective action of caveolin-1.Nature communications · 2026Article
- Article
- Adversarial Erasing Enhanced Multiple Instance Learning (siMILe): Discriminative Identification of Oligomeric Protein Structures in Single Molecule Localization Microscopy.Advanced intelligent systems (Weinheim an der Bergstrasse, Germany) · 2026Article
- Diffusing caveolin-1 scaffolds regulate mechanosignalling.Nature cell biology · 2026Article
- HDCluster: High-Degree Graph Clustering for Robust Analysis of Single Molecule Localization Microscopy.bioRxiv : the preprint server for biology · 2025Article
- Membrane Remodeling by the Collective Action of Caveolin-1.bioRxiv : the preprint server for biology · 2025Article
- SuperResNET: Model-Free Single-Molecule Network Analysis Software Achieves Molecular Resolution of Nup96.Advanced intelligent systems (Weinheim an der Bergstrasse, Germany) · 2025Article
- The role of Caveolin-1 in tumor-derived extracellular vesicle biology and its implications.Frontiers in cell and developmental biology · 2025Review
- MINFLUX fluorescence nanoscopy in biological tissue.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Lipid organization by the Caveolin-1 complex.Biophysical journal · 2024Article
- AI analysis of super-resolution microscopy: Biological discovery in the absence of ground truth.The Journal of cell biology · 2024Review
- Lipid Organization by the Caveolin-1 Complex.bioRxiv : the preprint server for biology · 2024Article
- Scaffolds and the scaffolding domain: an alternative paradigm for caveolin-1 signaling.Biochemical Society transactions · 2024Review
- Article
- Caveolin-1: A Review of Intracellular Functions, Tissue-Specific Roles, and Epithelial Tight Junction Regulation.Biology · 2023Review
- Early proteostasis of caveolins synchronizes trafficking, degradation, and oligomerization to prevent toxic aggregation.The Journal of cell biology · 2023Article
- Template-free prediction of a new monotopic membrane protein fold and assembly by AlphaFold2.Biophysical journal · 2023Article
- The building blocks of caveolae revealed: caveolins finally take center stage.Biochemical Society transactions · 2023Article
- Caveolin-1 in Müller Glia Exists as Heat-Resistant, High Molecular Weight Complexes.Advances in experimental medicine and biology · 2023Article
- A deep learning-based tool for the automated detection and analysis of caveolae in transmission electron microscopy images.Computational and structural biotechnology journal · 2023Article
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5 authors.
Funding
Abstract
Caveolin-1 (Cav1), the coat protein for caveolae, also forms non-caveolar Cav1 scaffolds. Single molecule Cav1 super-resolution microscopy analysis previously identified caveolae and three distinct scaffold domains: smaller S1A and S2B scaffolds and larger hemispherical S2 scaffolds. Application here of network modularity analysis of SMLM data for endogenous Cav1 labeling in HeLa cells shows that small scaffolds combine to form larger scaffolds and caveolae. We find modules within Cav1 blobs by maximizing the intra-connectivity between Cav1 molecules within a module and minimizing the inter-connectivity between Cav1 molecules across modules, which is achieved via spectral decomposition of the localizations adjacency matrix. Features of modules are then matched with intact blobs to find the similarity between the module-blob pairs of group centers. Our results show that smaller S1A and S1B scaffolds are made up of small polygons, that S1B scaffolds correspond to S1A scaffold dimers and that caveolae and hemispherical S2 scaffolds are complex, modular structures formed from S1B and S1A scaffolds, respectively. Polyhedral interactions of Cav1 oligomers, therefore, leads progressively to the formation of larger and more complex scaffold domains and the biogenesis of caveolae.
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