ArticleProceedings of the National Academy of Sciences of the United States of America2024
Structure of the flotillin complex in a native membrane environment.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed.
- The Arabidopsis SPFH protein HIR2 modulates receptor signaling and plasma membrane organization.The EMBO journal · 2026Article
- Molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2.Nature communications · 2026Article
- Structural insights into the organization of the human Erlin complex.Journal of molecular cell biology · 2026Article
- Structural basis for prohibitin-mediated regulation of mitochondrial m-AAA protease.Nature communications · 2026Article
- Structural flexibility of the human vault particle revealed by high-resolution cryo-EM and molecular dynamics simulations.Nature communications · 2026Article
- Structural energetics of cold sensitivity.Nature · 2026Article
- Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2.The Plant journal : for cell and molecular biology · 2026Article
- Article
- The vault associates with membranes in situ.Nature communications · 2026Article
- Structural plasticity of the membrane-bound protein degradation assembly supports bacterial adaptation to stress.Cell reports · 2026Article
- Stomatin encapsulates aquaporin-1 and urea transporter-B in the erythrocyte membrane.Science advances · 2026Article
- Exploring the Diversity and Function of the SPFH-Domain Containing Proteins in Pseudomonas aeruginosa.Environmental microbiology reports · 2026Article
- The vault particle is enclosed by aScience advances · 2026Article
- Structure first - exploration and discovery with cryo-electron microscopy.Journal of cell science · 2026Review
- Molecular mechanisms of flotillin complexes in organizing membrane microdomains.Nature communications · 2026Article
- Cathepsin-dependent amyloid formation drives mechanical rupture of lysosomal membranes.bioRxiv : the preprint server for biology · 2026Article
- Membrane microdomains are crucial forScience advances · 2026Article
- Direct Profiling of Extracellular Vesicle Surface Markers in Plasma: A Proof-of-Concept Study.Biology of the cell · 2025Article
- Structures of human organellar SPFH protein complexes.Nature communications · 2025Article
- In situ structure of a gap junction-stomatin complex.Science advances · 2025Article
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Abstract
In this study, we used cryoelectron microscopy to determine the structures of the Flotillin protein complex, part of the Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) superfamily, from cell-derived vesicles without detergents. It forms a right-handed helical barrel consisting of 22 pairs of Flotillin1 and Flotillin2 subunits, with a diameter of 32 nm at its wider end and 19 nm at its narrower end. Oligomerization is stabilized by the C terminus, which forms two helical layers linked by a β-strand, and coiled-coil domains that enable strong charge-charge intersubunit interactions. Flotillin interacts with membranes at both ends; through its SPFH1 domains at the wide end and the C terminus at the narrow end, facilitated by hydrophobic interactions and lipidation. The inward tilting of the SPFH domain, likely triggered by phosphorylation, suggests its role in membrane curvature induction, which could be connected to its proposed role in clathrin-independent endocytosis. The structure suggests a shared architecture across the family of SPFH proteins and will promote further research into Flotillin's roles in cell biology.
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