ArticleProceedings of the National Academy of Sciences of the United States of America2002
Mechanism of caveolin filament assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Stomatocyte-discocyte-echinocyte transformations of erythrocyte modulated by membrane-cytoskeleton mechanical properties.Biophysical journal · 2025Article
- Alpha-hemolysin promotes internalization of Staphylococcus aureus into human lung epithelial cells via caveolin-1- and cholesterol-rich lipid rafts.Cellular and molecular life sciences : CMLS · 2024Article
- Scaffolds and the scaffolding domain: an alternative paradigm for caveolin-1 signaling.Biochemical Society transactions · 2024Review
- One-step site-specific S-alkylation of full-length caveolin-1: Lipidation modulates the topology of its C-terminal domain.Protein science : a publication of the Protein Society · 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
- Redox Regulation of Signaling Complex between Caveolin-1 and Neuronal Calcium Sensor Recoverin.Biomolecules · 2022Article
- Emerging Insights into the Molecular Architecture of Caveolin-1.The Journal of membrane biology · 2022Review
- Caveolin-3 and Arrhythmias: Insights into the Molecular Mechanisms.Journal of clinical medicine · 2022Review
- Exploring the eukaryotic Yip and REEP/Yop superfamily of membrane-shaping adapter proteins (MSAPs): A cacophony or harmony of structure and function?Frontiers in molecular biosciences · 2022Review
- Reconstitution of Caveolin-1 into Artificial Lipid Membrane: Characterization by Transmission Electron Microscopy and Solid-State Nuclear Magnetic Resonance.Molecules (Basel, Switzerland) · 2021Article
- Structural Interplays in the Flexible N-Terminus and Scaffolding Domain of Human Membrane Protein Caveolin 3.Membranes · 2021Article
- Structure and assembly of CAV1 8S complexes revealed by single particle electron microscopy.Science advances · 2020Article
- Reconstitution of full-length human caveolin-1 into phospholipid bicelles: Validation by analytical ultracentrifugation.Biophysical chemistry · 2020Article
- The importance of caveolins and caveolae to dermatology: Lessons from the caves and beyond.Experimental dermatology · 2020Review
- Energy and Dynamics of Caveolae Trafficking.Frontiers in cell and developmental biology · 2020Review
- Live-Cell FRET Imaging of Phosphorylation-Dependent Caveolin-1 Switch.Methods in molecular biology (Clifton, N.J.) · 2020Article
- A junctophilin-caveolin interaction enables efficient coupling between ryanodine receptors and BKThe Journal of biological chemistry · 2019Article
- Cell Intrinsic and Extrinsic Mechanisms of Caveolin-1-Enhanced Metastasis.Biomolecules · 2019Review
- Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019Review
2 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Caveolin-1 was the first protein identified that colocalizes with the approximately 10-nm filaments found on the inside surface of caveolae membranes. We have used a combination of electron microscopy (EM), circular dichroism, and analytical ultracentrifugation to determine the structure of the oligomers that form when the first 101 aa of caveolin-1 (Cav(1-101)) are allowed to associate. We determined that amino acids 79-96 in this caveolin-1 fragment are arranged in an alpha-helix. Cav(1-101) oligomers are approximately 11 nm in diameter and contain seven molecules of Cav(1-101). These subunits, in turn, are able to assemble into 50 nm long x 11 nm diameter filaments that closely match the morphology of the filaments in the caveolae filamentous coat. We propose that the heptameric subunit forms in part through lateral interactions between the alpha-helices of the seven Cav(1-101) units. Caveolin-1, therefore, appears to be the structural molecule of the caveolae filamentous coat.
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