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| | <StructureSection load='6o3e' size='340' side='right'caption='[[6o3e]], [[Resolution|resolution]] 4.00Å' scene=''> | | <StructureSection load='6o3e' size='340' side='right'caption='[[6o3e]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o3e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O3E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o3e]] 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=6O3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O3E FirstGlance]. <br> |
| - | </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=6o3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o3e OCA], [http://pdbe.org/6o3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o3e RCSB], [http://www.ebi.ac.uk/pdbsum/6o3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o3e ProSAT]</span></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]] 4.001Å</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=6o3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o3e OCA], [https://pdbe.org/6o3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o3e RCSB], [https://www.ebi.ac.uk/pdbsum/6o3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o3e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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/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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6o3e" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6o3e" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Catenin 3D structures|Catenin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pokutta, S]] | + | [[Category: Mus musculus]] |
| - | [[Category: Weis, W I]] | + | [[Category: Pokutta S]] |
| - | [[Category: Actin binding]] | + | [[Category: Weis WI]] |
| - | [[Category: Catenin]]
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| - | [[Category: Cell adhesion]]
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| Structural highlights
Function
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.[1]
Publication Abstract from PubMed
Adherens Junctions (AJs) are cell-cell adhesion complexes that sense and propagate mechanical forces by coupling cadherins to the actin cytoskeleton via beta-catenin and the F-actin binding protein alphaE-catenin. When subjected to mechanical force, the cadherin*catenin complex can tightly link to F-actin through alphaE-catenin, and also recruits the F-actin-binding protein vinculin. In this study, labeling of native cysteines combined with mass spectrometry revealed conformational changes in alphaE-catenin upon binding to the E-cadherin*beta-catenin complex, vinculin and F-actin. A method to apply physiologically meaningful forces in solution revealed force-induced conformational changes in alphaE-catenin when bound to F-actin. Comparisons of wild-type alphaE-catenin and a mutant with enhanced vinculin affinity using cysteine labeling and isothermal titration calorimetry provide evidence for allosteric coupling of the N-terminal beta-catenin-binding and the middle (M) vinculin-binding domain of alphaE-catenin. Cysteine labeling also revealed possible crosstalk between the actin-binding domain and the rest of the protein. The data provide insight into how binding partners and mechanical stress can regulate the conformation of full-length alphaE-catenin, and identify the M domain as a key transmitter of conformational changes.
Binding partner- and force-promoted changes in alphaE-catenin conformation probed by native cysteine labeling.,Terekhova K, Pokutta S, Kee YS, Li J, Tajkhorshid E, Fuller G, Dunn AR, Weis WI Sci Rep. 2019 Oct 25;9(1):15375. doi: 10.1038/s41598-019-51816-3. PMID:31653927[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI. Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell. 2005 Dec 2;123(5):903-15. PMID:16325583 doi:10.1016/j.cell.2005.09.021
- ↑ Terekhova K, Pokutta S, Kee YS, Li J, Tajkhorshid E, Fuller G, Dunn AR, Weis WI. Binding partner- and force-promoted changes in alphaE-catenin conformation probed by native cysteine labeling. Sci Rep. 2019 Oct 25;9(1):15375. doi: 10.1038/s41598-019-51816-3. PMID:31653927 doi:http://dx.doi.org/10.1038/s41598-019-51816-3
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