http://purl.uniprot.org/citations/36928388 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/36928388 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.org/dc/terms/identifier | "doi:10.1038/s42003-023-04610-x"xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/author | "Smith E.W."xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/author | "Rangarajan E.S."xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/author | "Izard T."xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/date | "2023"xsd:gYear |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/name | "Commun Biol"xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/pages | "276"xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/title | "Distinct inter-domain interactions of dimeric versus monomeric alpha-catenin link cell junctions to filaments."xsd:string |
http://purl.uniprot.org/citations/36928388 | http://purl.uniprot.org/core/volume | "6"xsd:string |
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