9BQ2

Structure of the flotillin complex in a native membrane environment

9BQ2 の概要

• エントリーDOI: 10.2210/pdb9bq2/pdb
• EMDBエントリー: 44792
• 分子名称: Flotillin-2, Flotillin-1 (2 entities in total)
• 機能のキーワード: flotillin complex, spfh, membrane interaction, endocytosis, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91452.77

構造登録者

Fu, Z.,MacKinnon, R. (登録日: 2024-05-08, 公開日: 2024-07-24)

主引用文献

Fu, Z.,MacKinnon, R.
Structure of the flotillin complex in a native membrane environment.
Proc.Natl.Acad.Sci.USA, 121:e2409334121-e2409334121, 2024

PubMed 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.

PubMed: 38985763
DOI: 10.1073/pnas.2409334121

実験手法

ELECTRON MICROSCOPY (3.5 Å)