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| | ==Crystal structure of the alphaN-catenin actin-binding domain== | | ==Crystal structure of the alphaN-catenin actin-binding domain== |
| - | <StructureSection load='4k1o' size='340' side='right' caption='[[4k1o]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='4k1o' size='340' side='right'caption='[[4k1o]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4k1o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K1O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K1O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k1o]] is a 1 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=4K1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K1O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k1n|4k1n]]</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=4k1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1o OCA], [https://pdbe.org/4k1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k1o RCSB], [https://www.ebi.ac.uk/pdbsum/4k1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1o ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Catna2, Ctnna2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4k1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k1o OCA], [http://pdbe.org/4k1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k1o RCSB], [http://www.ebi.ac.uk/pdbsum/4k1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k1o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE]] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref> | + | [https://www.uniprot.org/uniprot/CTNA2_MOUSE CTNA2_MOUSE] May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.<ref>PMID:12089526</ref> <ref>PMID:12123610</ref> <ref>PMID:15034585</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Catenin|Catenin]] | + | *[[Catenin 3D structures|Catenin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Ikura, M]] | + | [[Category: Mus musculus]] |
| - | [[Category: Ishiyama, N]] | + | [[Category: Ikura M]] |
| - | [[Category: Alpha-catenin]] | + | [[Category: Ishiyama N]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: F-actin]]
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| - | [[Category: Five-helix bundle]]
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| Structural highlights
Function
CTNA2_MOUSE May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system. Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation.[1] [2] [3]
Publication Abstract from PubMed
alpha-catenin is an actin- and vinculin-binding protein that regulates cell-cell adhesion by interacting with cadherin adhesion receptors through beta-catenin, but the mechanisms by which it anchors the cadherin-catenin complex to the actin cytoskeleton at adherens junctions remain unclear. Here we determined crystal structures of alphaE-catenin in the autoinhibited state and the actin-binding domain of alphaN-catenin. Together with the small-angle X-ray scattering analysis of full-length alphaN-catenin, we deduced an elongated multidomain assembly of monomeric alpha-catenin that structurally and functionally couples the vinculin- and actin-binding mechanisms. Cellular and biochemical studies of alphaE- and alphaN-catenins show that alphaE-catenin recruits vinculin to adherens junctions more effectively than alphaN-catenin, partly owing to its higher affinity for actin filaments. We propose a molecular switch mechanism involving multi-state conformational changes of alpha-catenin. This would be driven by actomyosin-generated tension to dynamically regulate the vinculin-assisted linkage between adherens junctions and the actin cytoskeleton.
An Autoinhibited Structure of alpha-catenin and Its Implications for Vinculin Recruitment to Adherens Junctions.,Ishiyama N, Tanaka N, Abe K, Yang YJ, Abbas YM, Umitsu M, Nagar B, Bueler SA, Rubinstein JL, Takeichi M, Ikura M J Biol Chem. 2013 Apr 15. PMID:23589308[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Park C, Falls W, Finger JH, Longo-Guess CM, Ackerman SL. Deletion in Catna2, encoding alpha N-catenin, causes cerebellar and hippocampal lamination defects and impaired startle modulation. Nat Genet. 2002 Jul;31(3):279-84. Epub 2002 Jun 24. PMID:12089526 doi:10.1038/ng908
- ↑ Togashi H, Abe K, Mizoguchi A, Takaoka K, Chisaka O, Takeichi M. Cadherin regulates dendritic spine morphogenesis. Neuron. 2002 Jul 3;35(1):77-89. PMID:12123610
- ↑ Abe K, Chisaka O, Van Roy F, Takeichi M. Stability of dendritic spines and synaptic contacts is controlled by alpha N-catenin. Nat Neurosci. 2004 Apr;7(4):357-63. Epub 2004 Mar 21. PMID:15034585 doi:10.1038/nn1212
- ↑ Ishiyama N, Tanaka N, Abe K, Yang YJ, Abbas YM, Umitsu M, Nagar B, Bueler SA, Rubinstein JL, Takeichi M, Ikura M. An Autoinhibited Structure of alpha-catenin and Its Implications for Vinculin Recruitment to Adherens Junctions. J Biol Chem. 2013 Apr 15. PMID:23589308 doi:10.1074/jbc.M113.453928
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