3ifq
From Proteopedia
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{{STRUCTURE_3ifq| PDB=3ifq | SCENE= }} | {{STRUCTURE_3ifq| PDB=3ifq | SCENE= }} | ||
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===Interction of plakoglobin and beta-catenin with desmosomal cadherins=== | ===Interction of plakoglobin and beta-catenin with desmosomal cadherins=== | ||
| + | {{ABSTRACT_PUBMED_19759396}} | ||
| - | + | ==Disease== | |
| + | [[http://www.uniprot.org/uniprot/PLAK_HUMAN PLAK_HUMAN]] Defects in JUP are the cause of Naxos disease (NXD) [MIM:[http://omim.org/entry/601214 601214]]. NXD is an autosomal recessive disorder combining diffuse non-epidermolytic palmoplantar keratoderma with arrhythmogenic right ventricular dysplasia/cardiomyopathy and woolly hair.<ref>PMID:10902626</ref> Defects in JUP are the cause of familial arrhythmogenic right ventricular dysplasia type 12 (ARVD12) [MIM:[http://omim.org/entry/611528 611528]]; also called arrhythmogenic right ventricular cardiomyopathy 12 (ARVC12). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall.<ref>PMID:10902626</ref><ref>PMID:17924338</ref><ref>PMID:20031617</ref> | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/PLAK_HUMAN PLAK_HUMAN]] Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity). [[http://www.uniprot.org/uniprot/CADH1_MOUSE CADH1_MOUSE]] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity). | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:019759396</ref><references group="xtra"/> | + | <ref group="xtra">PMID:019759396</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
Revision as of 00:44, 25 March 2013
Contents |
Interction of plakoglobin and beta-catenin with desmosomal cadherins
Template:ABSTRACT PUBMED 19759396
Disease
[PLAK_HUMAN] Defects in JUP are the cause of Naxos disease (NXD) [MIM:601214]. NXD is an autosomal recessive disorder combining diffuse non-epidermolytic palmoplantar keratoderma with arrhythmogenic right ventricular dysplasia/cardiomyopathy and woolly hair.[1] Defects in JUP are the cause of familial arrhythmogenic right ventricular dysplasia type 12 (ARVD12) [MIM:611528]; also called arrhythmogenic right ventricular cardiomyopathy 12 (ARVC12). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall.[2][3][4]
Function
[PLAK_HUMAN] Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity). [CADH1_MOUSE] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity).
About this Structure
3ifq is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
See Also
Reference
- Choi HJ, Gross JC, Pokutta S, Weis WI. Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes. J Biol Chem. 2009 Nov 13;284(46):31776-88. Epub 2009 Sep 16. PMID:19759396 doi:10.1074/jbc.M109.047928
- ↑ McKoy G, Protonotarios N, Crosby A, Tsatsopoulou A, Anastasakis A, Coonar A, Norman M, Baboonian C, Jeffery S, McKenna WJ. Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease). Lancet. 2000 Jun 17;355(9221):2119-24. PMID:10902626 doi:10.1016/S0140-6736(00)02379-5
- ↑ McKoy G, Protonotarios N, Crosby A, Tsatsopoulou A, Anastasakis A, Coonar A, Norman M, Baboonian C, Jeffery S, McKenna WJ. Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease). Lancet. 2000 Jun 17;355(9221):2119-24. PMID:10902626 doi:10.1016/S0140-6736(00)02379-5
- ↑ Asimaki A, Syrris P, Wichter T, Matthias P, Saffitz JE, McKenna WJ. A novel dominant mutation in plakoglobin causes arrhythmogenic right ventricular cardiomyopathy. Am J Hum Genet. 2007 Nov;81(5):964-73. Epub 2007 Sep 28. PMID:17924338 doi:10.1086/521633
- ↑ den Haan AD, Tan BY, Zikusoka MN, Llado LI, Jain R, Daly A, Tichnell C, James C, Amat-Alarcon N, Abraham T, Russell SD, Bluemke DA, Calkins H, Dalal D, Judge DP. Comprehensive desmosome mutation analysis in north americans with arrhythmogenic right ventricular dysplasia/cardiomyopathy. Circ Cardiovasc Genet. 2009 Oct;2(5):428-35. doi:, 10.1161/CIRCGENETICS.109.858217. Epub 2009 Jun 3. PMID:20031617 doi:10.1161/CIRCGENETICS.109.858217
Categories: Homo sapiens | Mus musculus | Choi, H J. | Gross, J C. | Pokutta, S. | Weis, W I. | Armadillo repeat | Cardiomyopathy | Cell adhesion | Cell junction | Cell membrane | Cleavage on pair of basic residue | Cytoskeleton | Disease mutation | Disulfide bond | Glycoprotein | Membrane | Palmoplantar keratoderma | Phosphoprotein | Transmembrane
