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TitleMolecular mechanisms of flotillin complexes in organizing membrane microdomains.
Journal, issue, pagesNat Commun, Year 2026
Publish dateFeb 9, 2026
AuthorsMing-Ao Lu / Yunwen Qian / Liangwen Ma / Jinzhi Hong / Xiaopeng Li / Li Yu / Qiang Guo / Ning Gao /
PubMed AbstractFlotillin-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 ...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.
External linksNat Commun / PubMed:41663364
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution3.58 - 25.6 Å
Structure data

62785

9l3g

EMDB-62785, PDB-9l3g:
Structure of the flotillin complex
Method: EM (single particle) / Resolution: 3.58 Å

EMDB-67802: Structure of the flotillin complex in situ
Method: EM (subtomogram averaging) / Resolution: 25.6 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / SPFH protein family / scaffold protein / membrane compartmentalization / membrane microdomain

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