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- PDB-7utj: Cryogenic electron microscopy 3D map of F-actin bound by human di... -
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Basic information
Entry | Database: PDB / ID: 7utj | ||||||
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Title | Cryogenic electron microscopy 3D map of F-actin bound by human dimeric alpha-catenin | ||||||
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![]() | CELL ADHESION / alpha-catenin / F-actin / F-actin binding protein / cell-cell junction | ||||||
Function / homology | ![]() negative regulation of integrin-mediated signaling pathway / CDH11 homotypic and heterotypic interactions / Regulation of CDH19 Expression and Function / Regulation of CDH11 function / gamma-catenin binding / epithelial cell-cell adhesion / zonula adherens / gap junction assembly / cellular response to indole-3-methanol / vinculin binding ...negative regulation of integrin-mediated signaling pathway / CDH11 homotypic and heterotypic interactions / Regulation of CDH19 Expression and Function / Regulation of CDH11 function / gamma-catenin binding / epithelial cell-cell adhesion / zonula adherens / gap junction assembly / cellular response to indole-3-methanol / vinculin binding / flotillin complex / negative regulation of cell motility / apical junction assembly / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of smoothened signaling pathway / Adherens junctions interactions / catenin complex / negative regulation of protein localization to nucleus / axon regeneration / cytoskeletal motor activator activity / negative regulation of neuroblast proliferation / smoothened signaling pathway / establishment or maintenance of cell polarity / Myogenesis / tropomyosin binding / mesenchyme migration / troponin I binding / myosin heavy chain binding / odontogenesis of dentin-containing tooth / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle myofibril / intercalated disc / actin monomer binding / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / neuroblast proliferation / RHO GTPases activate IQGAPs / skeletal muscle fiber development / stress fiber / ovarian follicle development / titin binding / extrinsic apoptotic signaling pathway in absence of ligand / actin filament polymerization / acrosomal vesicle / VEGFR2 mediated vascular permeability / filopodium / integrin-mediated signaling pathway / actin filament / adherens junction / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / protein localization / beta-catenin binding / cell-cell adhesion / response to estrogen / calcium-dependent protein binding / male gonad development / cell-cell junction / actin filament binding / cell migration / actin cytoskeleton / lamellipodium / cell junction / cell body / hydrolase activity / cell adhesion / cadherin binding / protein domain specific binding / intracellular membrane-bounded organelle / focal adhesion / calcium ion binding / positive regulation of gene expression / structural molecule activity / magnesium ion binding / RNA binding / ATP binding / identical protein binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.77 Å | ||||||
![]() | Rangarajan, E.S. / Smith, E.W. / Izard, T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Distinct inter-domain interactions of dimeric versus monomeric α-catenin link cell junctions to filaments. Authors: Erumbi S Rangarajan / Emmanuel W Smith / Tina Izard / ![]() 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 ...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. | ||||||
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-Validation report
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Data in XML | ![]() | 94.7 KB | Display | |
Data in CIF | ![]() | 137.5 KB | Display | |
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-Related structure data
Related structure data | ![]() 26772MC ![]() 7uxfC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Noncrystallographic symmetry (NCS) | NCS domain:
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