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-Structure paper
タイトル | Molecular mechanism for direct actin force-sensing by α-catenin. |
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ジャーナル・号・ページ | Elife, Vol. 9, Year 2020 |
掲載日 | 2020年9月24日 |
著者 | Lin Mei / Santiago Espinosa de Los Reyes / Matthew J Reynolds / Rachel Leicher / Shixin Liu / Gregory M Alushin / |
PubMed 要旨 | The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear ...The actin cytoskeleton mediates mechanical coupling between cells and their tissue microenvironments. The architecture and composition of actin networks are modulated by force; however, it is unclear how interactions between actin filaments (F-actin) and associated proteins are mechanically regulated. Here we employ both optical trapping and biochemical reconstitution with myosin motor proteins to show single piconewton forces applied solely to F-actin enhance binding by the human version of the essential cell-cell adhesion protein αE-catenin but not its homolog vinculin. Cryo-electron microscopy structures of both proteins bound to F-actin reveal unique rearrangements that facilitate their flexible C-termini refolding to engage distinct interfaces. Truncating α-catenin's C-terminus eliminates force-activated F-actin binding, and addition of this motif to vinculin confers force-activated binding, demonstrating that α-catenin's C-terminus is a modular detector of F-actin tension. Our studies establish that piconewton force on F-actin can enhance partner binding, which we propose mechanically regulates cellular adhesion through α-catenin. |
リンク | Elife / PubMed:32969337 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.9 - 3.2 Å |
構造データ | EMDB-20843, PDB-6upv: EMDB-20844, PDB-6upw: |
化合物 | ChemComp-ADP: ChemComp-MG: |
由来 |
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キーワード | CELL ADHESION / alpha-catenin / catenin / actin / mechanobiology / mechanosensing / cytoskeleton / vinculin / metavinculin / focal adhesion |