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-Structure paper
| タイトル | High-resolution snapshots of the talin auto-inhibitory states suggest roles in cell adhesion and signaling. |
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| ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 9270, Year 2024 |
| 掲載日 | 2024年10月28日 |
著者 | Erumbi S Rangarajan / Julian L Bois / Scott B Hansen / Tina Izard / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:39468080 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.7 - 5.5 Å |
| 構造データ | EMDB-43152, PDB-8vdo: EMDB-43154, PDB-8vdp: EMDB-43155, PDB-8vdq: EMDB-43156, PDB-8vdr: ![]() EMDB-44931: Cryogenic electron microscopy model of talin with alternate FABD conformation |
| 由来 |
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キーワード | CELL ADHESION / Talin / focal adhesion / f-actin binding |
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