6UPW
Metavinculin ABD-F-actin complex
Summary for 6UPW
| Entry DOI | 10.2210/pdb6upw/pdb |
| Related | 6upv |
| EMDB information | 20843 20844 |
| Descriptor | Vinculin, Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | vinculin, metavinculin, actin, mechanobiology, mechanosensing, cytoskeleton, cell adhesion, focal adhesion |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 7 |
| Total formula weight | 459548.45 |
| Authors | Mei, L.,Alushin, G.M. (deposition date: 2019-10-18, release date: 2020-09-30, Last modification date: 2025-04-02) |
| Primary citation | Mei, L.,Espinosa de Los Reyes, S.,Reynolds, M.J.,Leicher, R.,Liu, S.,Alushin, G.M. Molecular mechanism for direct actin force-sensing by alpha-catenin. Elife, 9:-, 2020 Cited by PubMed Abstract: 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. PubMed: 32969337DOI: 10.7554/eLife.62514 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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