7UXF
Cryogenic electron microscopy 3D map of F-actin
Summary for 7UXF
| Entry DOI | 10.2210/pdb7uxf/pdb |
| EMDB information | 26772 26860 |
| Descriptor | Actin, alpha skeletal muscle, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | f-actin, cell-cell junction, cell adhesion |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 6 |
| Total formula weight | 255368.87 |
| Authors | Rangarajan, E.S.,Smith, E.W.,Izard, T. (deposition date: 2022-05-05, release date: 2023-03-08, Last modification date: 2023-03-29) |
| Primary citation | Rangarajan, E.S.,Smith, E.W.,Izard, T. Distinct inter-domain interactions of dimeric versus monomeric alpha-catenin link cell junctions to filaments. Commun Biol, 6:276-276, 2023 Cited by PubMed Abstract: Attachment between cells is crucial for almost all aspects of the life of cells. These inter-cell adhesions are mediated by the binding of transmembrane cadherin receptors of one cell to cadherins of a neighboring cell. Inside the cell, cadherin binds β-catenin, which interacts with α-catenin. The transitioning of cells between migration and adhesion is modulated by α-catenin, which links cell junctions and the plasma membrane to the actin cytoskeleton. At cell junctions, a single β-catenin/α-catenin heterodimer slips along filamentous actin in the direction of cytoskeletal tension which unfolds clustered heterodimers to form catch bonds with F-actin. Outside cell junctions, α-catenin dimerizes and links the plasma membrane to F-actin. Under cytoskeletal tension, α-catenin unfolds and forms an asymmetric catch bond with F-actin. To understand the mechanism of this important α-catenin function, we determined the 2.7 Å cryogenic electron microscopy (cryoEM) structures of filamentous actin alone and bound to human dimeric α-catenin. Our structures provide mechanistic insights into the role of the α-catenin interdomain interactions in directing α-catenin function and suggest a bivalent mechanism. Further, our cryoEM structure of human monomeric α-catenin provides mechanistic insights into α-catenin autoinhibition. Collectively, our structures capture the initial α-catenin interaction with F-actin before the sensing of force, which is a crucial event in cell adhesion and human disease. PubMed: 36928388DOI: 10.1038/s42003-023-04610-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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