ArticleNature communications2026
Molecular mechanisms of flotillin complexes in organizing membrane microdomains.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed.
- Disruption of Functional Membrane Microdomains Enhances Methicillin-ResistantVeterinary sciences · 2026Article
- Microplastics as Vectors Influencing Oxidative Stress, Inflammation, and Endocrine Function During Early Development.International journal of molecular sciences · 2026Review
- Structural basis for prohibitin-mediated regulation of mitochondrial m-AAA protease.Nature communications · 2026Article
- The vault associates with membranes in situ.Nature communications · 2026Article
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Authors and funding
8 authors.
Funding
Abstract
Flotillin-1 and flotillin-2 form hetero-oligomers to create flotillin membrane microdomains essential for endocytosis and protein sorting. However, the mechanisms of flotillin oligomerization and microdomain organization remain incompletely understood. Here, we present the cryo-EM structure of human flotillin complex, showing that flotillin-1 and -2 form a 44-mer, membrane attached, and dome-shaped structure that defines a 30-nm circular membrane domain. The cryo-ET data demonstrates that while attached to the cytoplasmic leaflet, flotillin complexes possess intrinsic structural plasticity in situ on the native membrane. Each flotillin complex may represent a fundamental unit of membrane microdomains, with their clustering enabling the formation of larger and more elaborate domains. We further reveal that phosphorylation at residues Y160 (flotillin-1) and Y163 (flotillin-2) may act as a molecular switch to modulate complex assembly, potentially regulating its function in endocytosis. These findings demonstrate the molecular mechanism of flotillin-mediated membrane segregation and microdomain formation, and suggest a previously unrecognized role of flotillin in sequestrating membrane proteins.
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