Summary for 9L3G
| Entry DOI | 10.2210/pdb9l3g/pdb |
| EMDB information | 62785 |
| Descriptor | Flotillin-1, Flotillin-2 (2 entities in total) |
| Functional Keywords | spfh protein family, scaffold protein, membrane compartmentalization, membrane microdomain, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 44 |
| Total formula weight | 2168901.61 |
| Authors | |
| Primary citation | Lu, M.A.,Qian, Y.,Ma, L.,Hong, J.,Li, X.,Yu, L.,Guo, Q.,Gao, N. Molecular mechanisms of flotillin complexes in organizing membrane microdomains. Nat Commun, 2026 Cited by PubMed 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. PubMed: 41663364DOI: 10.1038/s41467-026-69197-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.58 Å) |
Structure validation
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