9dva: Difference between revisions
New page: '''Unreleased structure''' The entry 9dva is ON HOLD Authors: Description: Category: Unreleased Structures |
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==F-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin== | |||
<StructureSection load='9dva' size='340' side='right'caption='[[9dva]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9dva]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DVA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9dva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dva OCA], [https://pdbe.org/9dva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dva RCSB], [https://www.ebi.ac.uk/pdbsum/9dva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dva ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ACTS_CHICK ACTS_CHICK] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The E-cadherin-beta-catenin-alphaE-catenin (cadherin-catenin) complex couples the cytoskeletons of neighboring cells at adherens junctions (AJs) to mediate force transmission across epithelia. Mechanical force and auxiliary binding partners converge to stabilize the cadherin-catenin complex's inherently weak binding to actin filaments (F-actin) through unclear mechanisms. Here we show that afadin's coiled-coil (CC) domain and vinculin synergistically enhance the cadherin-catenin complex's F-actin engagement. The cryo-EM structure of an E-cadherin-beta-catenin-alphaE-catenin-vinculin-afadin-CC supra-complex bound to F-actin reveals that afadin-CC bridges adjacent alphaE-catenin actin-binding domains along the filament, stabilizing flexible alphaE-catenin segments implicated in mechanical regulation. These cooperative binding contacts promote the formation of supra-complex clusters along F-actin. Additionally, cryo-EM variability analysis links supra-complex binding along individual F-actin strands to nanoscale filament curvature, a deformation mode associated with cytoskeletal forces. Collectively, this work elucidates a mechanistic framework by which vinculin and afadin tune cadherin-catenin complex-cytoskeleton coupling to support AJ function across varying mechanical regimes. | |||
Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature.,Gong R, Reynolds MJ, Sun X, Alushin GM bioRxiv [Preprint]. 2024 Oct 11:2024.10.08.617332. doi: , 10.1101/2024.10.08.617332. PMID:39415991<ref>PMID:39415991</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9dva" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Alushin GM]] | |||
[[Category: Gong R]] | |||
[[Category: Reynolds MJ]] | |||
Latest revision as of 09:19, 30 October 2024
F-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadinF-actin binding interface of alpha-E-catenin ABD (cadherin-catenin complex) and afadin
Structural highlights
FunctionACTS_CHICK Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMedThe E-cadherin-beta-catenin-alphaE-catenin (cadherin-catenin) complex couples the cytoskeletons of neighboring cells at adherens junctions (AJs) to mediate force transmission across epithelia. Mechanical force and auxiliary binding partners converge to stabilize the cadherin-catenin complex's inherently weak binding to actin filaments (F-actin) through unclear mechanisms. Here we show that afadin's coiled-coil (CC) domain and vinculin synergistically enhance the cadherin-catenin complex's F-actin engagement. The cryo-EM structure of an E-cadherin-beta-catenin-alphaE-catenin-vinculin-afadin-CC supra-complex bound to F-actin reveals that afadin-CC bridges adjacent alphaE-catenin actin-binding domains along the filament, stabilizing flexible alphaE-catenin segments implicated in mechanical regulation. These cooperative binding contacts promote the formation of supra-complex clusters along F-actin. Additionally, cryo-EM variability analysis links supra-complex binding along individual F-actin strands to nanoscale filament curvature, a deformation mode associated with cytoskeletal forces. Collectively, this work elucidates a mechanistic framework by which vinculin and afadin tune cadherin-catenin complex-cytoskeleton coupling to support AJ function across varying mechanical regimes. Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature.,Gong R, Reynolds MJ, Sun X, Alushin GM bioRxiv [Preprint]. 2024 Oct 11:2024.10.08.617332. doi: , 10.1101/2024.10.08.617332. PMID:39415991[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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