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-Structure paper
タイトル | Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments. |
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ジャーナル・号・ページ | Commun Biol, Vol. 6, Issue 1, Page 276, Year 2023 |
掲載日 | 2023年3月16日 |
著者 | Erumbi S Rangarajan / Emmanuel W Smith / Tina Izard / |
PubMed 要旨 | 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 ...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. |
リンク | Commun Biol / PubMed:36928388 / PubMed Central |
手法 | EM (らせん対称) / EM (単粒子) |
解像度 | 2.7 - 6.9 Å |
構造データ | EMDB-26772, PDB-7utj: EMDB-26860, PDB-7uxf: EMDB-27717: Cryogenic electron microscopy 3D map of human full-length monomeric alpha-catenin |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-HOH: |
由来 |
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キーワード | CELL ADHESION / alpha-catenin / F-actin / F-actin binding protein / cell-cell junction |