9L3G

Structure of the flotillin complex

これはPDB形式変換不可エントリーです。

9L3G の概要

• エントリーDOI: 10.2210/pdb9l3g/pdb
• EMDBエントリー: 62785
• 分子名称: Flotillin-1, Flotillin-2 (2 entities in total)
• 機能のキーワード: spfh protein family, scaffold protein, membrane compartmentalization, membrane microdomain, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 44
• 化学式量合計: 2168901.61

構造登録者

Lu, M.,Gao, N. (登録日: 2024-12-18, 公開日: 2025-12-24, 最終更新日: 2026-04-01)

主引用文献

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, 17:-, 2026

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: 41663364
DOI: 10.1038/s41467-026-69197-3

実験手法

ELECTRON MICROSCOPY (3.58 Å)