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4ons

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Revision as of 22:02, 5 August 2016

Structural and thermodynamic characterization of cadherin-beta-catenin-alpha-catenin complex formation

Structural highlights

4ons is a 4 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Ctnna2, Catna2 (LK3 transgenic mice), Ctnnb1, Catnb (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [CTNB1_MOUSE] Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation of cell adhesion. Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (By similarity).

Publication Abstract from PubMed

The classical cadherin-beta-catenin-alpha-catenin complex mediates homophilic cell-cell adhesion and mechanically couples the actin cytoskeletons of adjacent cells. Although alpha-catenin binds to beta-catenin and to F-actin, beta-catenin significantly weakens the affinity of alpha-catenin for F-actin. Moreover, alpha-catenin self-associates into homodimers that block beta-catenin binding. We investigated quantitatively and structurally alphaE- and alphaN-catenin dimer formation, their interaction with beta-catenin and the cadherin-beta-catenin complex, and the effect of the alpha-catenin actin-binding domain on beta-catenin association. The two alpha-catenin variants differ in their self-association properties: at physiological temperatures alphaE-catenin homodimerizes 10x more weakly than does alphaN-catenin, but is kinetically trapped in its oligomeric state. Both alphaE- and alphaN-catenin bind to beta-catenin with a Kd of 20 nM, and this affinity is increased by an order of magnitude when cadherin is bound to beta-catenin. We describe the crystal structure of a complex representing the full beta-catenin-alphaN-catenin interface. A three-dimensional model of the cadherin-beta-catenin-alpha-catenin complex based on these new structural data suggests mechanisms for the enhanced stability of the ternary complex. The C-terminal actin-binding domain of alpha-catenin has no influence on the interactions with beta-catenin, arguing against models in which beta-catenin weakens actin binding by stabilizing inhibitory intramolecular interactions between the actin-binding domain and the rest of alpha-catenin.

Structural and Thermodynamic Characterization of Cadherin-beta-catenin-alpha-catenin Complex Formation.,Pokutta S, Choi HJ, Ahlsen G, Hansen SD, Weis WI J Biol Chem. 2014 Apr 1. PMID:24692547^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Pokutta S, Choi HJ, Ahlsen G, Hansen SD, Weis WI. Structural and Thermodynamic Characterization of Cadherin-beta-catenin-alpha-catenin Complex Formation. J Biol Chem. 2014 Apr 1. PMID:24692547 doi:http://dx.doi.org/10.1074/jbc.M114.554709

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ons"

@@ Line 1: / Line 1: @@
 ==Structural and thermodynamic characterization of cadherin-beta-catenin-alpha-catenin complex formation==
 <StructureSection load='4ons' size='340' side='right' caption='[[4ons]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4ons]] is a 4 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=4ONS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ONS FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ctnna2, Catna2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Ctnnb1, Catnb ([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=4ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ons OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ons RCSB], [http://www.ebi.ac.uk/pdbsum/4ons PDBsum]</span></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=4ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ons OCA], [http://pdbe.org/4ons PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ons RCSB], [http://www.ebi.ac.uk/pdbsum/4ons PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ons ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ons" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Catenin|Catenin]]
 == References ==
 <references/>

4ons

From Proteopedia

Revision as of 22:02, 5 August 2016

Structural and thermodynamic characterization of cadherin-beta-catenin-alpha-catenin complex formation

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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