8VDO

Cryogenic electron microscopy model of full-length talin lacking F2, R12 and FABD.

8VDO の概要

• エントリーDOI: 10.2210/pdb8vdo/pdb
• EMDBエントリー: 43152 43154 43155 43156 44931
• 分子名称: Green fluorescent protein,Talin-1 (1 entity in total)
• 機能のキーワード: talin, focal adhesion, f-actin binding, cell adhesion
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 299867.34

構造登録者

Izard, T.,Rangarajan, E.S. (登録日: 2023-12-16, 公開日: 2024-10-02, 最終更新日: 2025-08-06)

主引用文献

Rangarajan, E.S.,Bois, J.L.,Hansen, S.B.,Izard, T.
High-resolution snapshots of the talin auto-inhibitory states suggest roles in cell adhesion and signaling.
Nat Commun, 15:9270-9270, 2024

PubMed Abstract: Talin regulates crucial cellular functions, including cell adhesion and motility, and affects human diseases. Triggered by mechanical forces, talin plays crucial roles in facilitating the formation of focal adhesions and recruiting essential focal adhesion regulatory elements such as vinculin. The structural flexibility allows talin to fine-tune its signaling responses. This study presents our 2.7 Å cryoEM structures of talin, which surprisingly uncovers several auto-inhibitory states. Contrary to previous suggestions, our structures reveal that (1) the first and last three domains are not involved in maintaining talin in its closed state and are mobile, (2) the talin F-actin and membrane binding domain are loosely attached and thus available for binding, and (3) the main force-sensing domain is oriented with its vinculin binding sites ready for release. These structural snapshots offer insights and advancements in understanding the dynamic talin activation mechanism, which is crucial for mediating cell adhesion.

PubMed: 39468080
DOI: 10.1038/s41467-024-52581-2

実験手法

ELECTRON MICROSCOPY (2.7 Å)