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==Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin==
==Crystal Structure of the complex between the vinculin D1 domain and alphaE-catenin==
<StructureSection load='5y04' size='340' side='right' caption='[[5y04]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='5y04' size='340' side='right'caption='[[5y04]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5y04]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y04 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5y04]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y04 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3w3r|3w3r]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5y04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y04 OCA], [http://pdbe.org/5y04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y04 RCSB], [http://www.ebi.ac.uk/pdbsum/5y04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y04 ProSAT]</span></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=5y04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y04 OCA], [https://pdbe.org/5y04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y04 RCSB], [https://www.ebi.ac.uk/pdbsum/5y04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y04 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VINC_MOUSE VINC_MOUSE]] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion (By similarity).[UniProtKB:P18206]<ref>PMID:7568093</ref> [[http://www.uniprot.org/uniprot/CTNA1_MOUSE CTNA1_MOUSE]] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.<ref>PMID:16325583</ref> 
[https://www.uniprot.org/uniprot/VINC_MOUSE VINC_MOUSE] Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion (By similarity).[UniProtKB:P18206]<ref>PMID:7568093</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mechanotransduction by alpha-catenin facilitates the force-dependent development of adherens junctions (AJs) by recruiting vinculin to reinforce actin anchoring of AJs. The alpha-catenin mechanotransducing action is facilitated by its force-sensing device region that autoinhibits the vinculin-binding site 1 (VBS1). Here, we report the high-resolution structure of the force-sensing device region of alpha-catenin, which shows the autoinhibited form comprised of helix bundles E, F and G. The cryptic VBS1 is embedded into helix bundle E stabilized by direct interactions with the autoinhibitory region forming helix bundles F and G. Our molecular dissection study showed that helix bundles F and G are stable in solution in each isolated form, whereas helix bundle E that contains VBS1 is unstable and intrinsically disordered in solution in the isolated form. We successfully identified key residues mediating the autoinhibition and produced mutated alpha-catenins that display variable force sensitivity and autoinhibition. Using these mutants, we demonstrate both in vitro and in vivo that, in the absence of this stabilization, the helix bundle containing VBS1 would adopt an unfolded form, thus exposing VBS for vinculin binding. We provide evidence for importance of mechanotransduction with the intrinsic force sensitivity for vinculin recruitment to adherens junctions of epithelial cell sheets with mutated alpha-catenins.


The force-sensing device region of alpha-catenin is an intrinsically disordered segment in the absence of intramolecular stabilization of the autoinhibitory form.,Hirano Y, Amano Y, Yonemura S, Hakoshima T Genes Cells. 2018 Mar 15. doi: 10.1111/gtc.12578. PMID:29542234<ref>PMID:29542234</ref>
==See Also==
 
*[[Catenin 3D structures|Catenin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
*[[Vinculin 3D structures|Vinculin 3D structures]]
</div>
<div class="pdbe-citations 5y04" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hakoshima, T]]
[[Category: Large Structures]]
[[Category: Hirano, Y]]
[[Category: Mus musculus]]
[[Category: Adherens junction]]
[[Category: Hakoshima T]]
[[Category: Cell adhesion]]
[[Category: Hirano Y]]
[[Category: Cytoskeleton]]

Latest revision as of 13:21, 27 March 2024

Crystal Structure of the complex between the vinculin D1 domain and alphaE-cateninCrystal Structure of the complex between the vinculin D1 domain and alphaE-catenin

Structural highlights

5y04 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.85Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VINC_MOUSE Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion (By similarity).[UniProtKB:P18206][1]

See Also

References

  1. ↑ Coll JL, Ben-Ze'ev A, Ezzell RM, Rodriguez Fernandez JL, Baribault H, Oshima RG, Adamson ED. Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion. Proc Natl Acad Sci U S A. 1995 Sep 26;92(20):9161-5. PMID:7568093

5y04, resolution 2.85Å

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