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Wikipedia

Plakoglobin

Plakoglobin, also known as junction plakoglobin or gamma-catenin, is a protein that in humans is encoded by the JUP gene.[5] Plakoglobin is a member of the catenin protein family and homologous to β-catenin. Plakoglobin is a cytoplasmic component of desmosomes and adherens junctions structures located within intercalated discs of cardiac muscle that function to anchor sarcomeres and join adjacent cells in cardiac muscle. Mutations in plakoglobin are associated with arrhythmogenic right ventricular dysplasia.

JUP
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesJUP, ARVD12, CTNNG, DP3, DPIII, PDGB, PKGB, Plakoglobin, junction plakoglobin, PG
External IDsOMIM: 173325 MGI: 96650 HomoloGene: 1680 GeneCards: JUP
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_010593

RefSeq (protein)

NP_034723

Location (UCSC)Chr 17: 41.75 – 41.79 MbChr 11: 100.26 – 100.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Structure edit

Human plakoglobin is 81.7 kDa in molecular weight and 745 amino acids long.[6] The JUP gene contains 13 exons spanning 17 kb on chromosome 17q21.[7] Plakoglobin is a member of the catenin family, since it contains a distinct repeating amino acid motif called the armadillo repeat.[5] Plakoglobin is highly similar to β-catenin; both have 12 armadillo repeats as well as N-terminal and C-terminal globular domains of unknown structure.[8] Plakoglobin was originally identified as a component of desmosomes, where it can bind to the cadherin family member desmoglein I. Plakoglobin also associates with classical cadherins such as E-cadherin; in that context, it was called gamma-catenin. Plakoglobin forms distinct complexes with cadherins and desmosomal cadherins.

Function edit

Plakoglobin is a major cytoplasmic component of both desmosomes and adherens junctions, and is the only known constituent common to submembranous plaques in both of these structures,[9] which are located at the intercalated disc (ICD) of cardiomyocytes. Plakoglobin links cadherins to the actin cytoskeleton. Plakoglobin binds to conserved regions of desmoglein and desmocollin at intracellular catenin-binding sites to assemble desmosomes.[10][11]

Plakoglobin is essential for normal development of intercalated discs and stability of cardiac muscle. Transgenic mice homozygous for a null mutation of the JUP gene die around embryonic day 12 from substantial defects in adherens junctions and a lack of functional desmosomes in the heart.[12][13] Further studies showed that cardiac fibers obtained from JUP-null embryonic mice had decreased passive compliance albeit normal attachment of sarcomeres to adherens junctions.[14]

In additional studies, an inducible cardiac-specific plakoglobin knockout mice were generated. Transgenic mice displayed a similar phenotype as arrhythmogenic right ventricular cardiomyopathy patients, with loss of cardiomyocytes, fibrosis and cardiac dysfunction, as well as alterations in desmosome protein content and gap junction remodeling. Hearts also exhibited increases in β-catenin signaling.[15][16] Further investigations on the role of β-catenin and plakoglobin in the heart generated a double knockout of these two proteins. Mice exhibited cardiomyopathy, fibrosis, conduction abnormalities and sudden cardiac death, presumably via spontaneous lethal ventricular arrhythmias. Mice also showed a decrease in gap junction structures at intercalated discs.[17]

Intracellular plakoglobin expression is controlled by Wnt signaling and ubiquitin-proteasome-dependent degradation. Phosphorylation of N-terminal Serines by a “destruction complex” composed of glycogen synthase kinase 3β (GSK3β) and scaffold proteins adenomatous polyposis coli (APC) and axin targets plakoglobin for degradation.[18][19][20][31–33]. The phosphorylated motif is recognized by β-TrCP, a ubiquitin ligase that targets plakoglobin 26S proteasome-dependent degradation.[21] Plakoglobin is also O-glycosylated near its N-terminal destruction box.

Clinical significance edit

Mutation of the JUP gene encoding plakoglobin has been implicated as one of the causes of the cardiomyopathy known as arrhythmogenic right ventricular dysplasia (ARVD) or arrhythmogenic right ventricular cardiomyopathy; mutations in JUP specifically causes an autosomal recessive form referred to as Naxos disease.[22][23][24] This form of was first identified in a small cluster of families on the Greek island of Naxos. The phenotype of the Naxos disease variant of ARVD is unique in that it involves the hair and skin as well as the right ventricle. Affected individuals have kinky, wooly hair; there is also palmar and plantar erythema at birth that progresses to keratosis as the palms and soles of the feet are used in crawling and walking.[25][26][27] These findings co-segregate 100% with the development of ARVD by early adolescence.

It has become clear that ARVD/ARVC is a disease of the cardiac muscle desmosome; advances in molecular genetics have illuminated this notion.[28][29][30][31][32][33][34][35][36]

Studies investigating the role of plakoglobin in disease pathology have found that suppression of desmoplakin expression by siRNA led to the nuclear localization of plakoglobin, resulting in a reduction in Wnt signaling via Tcf/Lef1 and ensued pathogenesis of ARVC.[37] Specifically, adipogenic factor expression was induced and cardiac progenitor cells at the epicardium were differentiated to adipocytes.[38]

Non-invasive cardiac screening identified T-wave inversion, abnormalities in right ventricular wall motion, and frequent ventricular extrasystoles as sensitive and specific markers of a JUP mutation.[39] Additional studies have shown that immunohistochemical analysis of cardiac muscle desmosomal proteins is also a sensitive and specific diagnostic text for ARVD/ARVC.[40]

Abnormal distribution of plakoglobin due to mutations in genes encoding for Desmoglein 1 and 3 have also been implicated in Pemphigus vulgaris.[41][42]

Interactions edit

Plakoglobin has been shown to interact with:

See also edit

References edit

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  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000001552 – Ensembl, May 2017
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Further reading edit

  • Cowin P, Kapprell HP, Franke WW, Tamkun J, Hynes RO (Sep 1986). "Plakoglobin: a protein common to different kinds of intercellular adhering junctions". Cell. 46 (7): 1063–73. doi:10.1016/0092-8674(86)90706-3. PMID 3530498. S2CID 45332970.
  • Franke WW, Goldschmidt MD, Zimbelmann R, Mueller HM, Schiller DL, Cowin P (Jun 1989). "Molecular cloning and amino acid sequence of human plakoglobin, the common junctional plaque protein". Proceedings of the National Academy of Sciences of the United States of America. 86 (11): 4027–31. Bibcode:1989PNAS...86.4027F. doi:10.1073/pnas.86.11.4027. PMC 287381. PMID 2726765.
  • Mathur M, Goodwin L, Cowin P (May 1994). "Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin". The Journal of Biological Chemistry. 269 (19): 14075–80. doi:10.1016/S0021-9258(17)36756-X. PMID 8188687.
  • Beavon IR (Aug 2000). "The E-cadherin-catenin complex in tumour metastasis: structure, function and regulation". European Journal of Cancer. 36 (13 Spec No): 1607–20. doi:10.1016/S0959-8049(00)00158-1. PMID 10959047.
  • Wilson PD (Apr 2001). "Polycystin: new aspects of structure, function, and regulation". Journal of the American Society of Nephrology. 12 (4): 834–45. doi:10.1681/ASN.V124834. PMID 11274246.
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External links edit

  • GeneReviews/NCBI/NIH/UW entry on Arrhythmogenic Right Ventricular Dysplasia/Cardiomyopathy, Autosomal Dominant
  • OMIM entries on Arrhythmogenic Right Ventricular Dysplasia/Cardiomyopathy, Autosomal Dominant
  • gamma-Catenin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

plakoglobin, also, known, junction, plakoglobin, gamma, catenin, protein, that, humans, encoded, gene, member, catenin, protein, family, homologous, catenin, cytoplasmic, component, desmosomes, adherens, junctions, structures, located, within, intercalated, di. Plakoglobin also known as junction plakoglobin or gamma catenin is a protein that in humans is encoded by the JUP gene 5 Plakoglobin is a member of the catenin protein family and homologous to b catenin Plakoglobin is a cytoplasmic component of desmosomes and adherens junctions structures located within intercalated discs of cardiac muscle that function to anchor sarcomeres and join adjacent cells in cardiac muscle Mutations in plakoglobin are associated with arrhythmogenic right ventricular dysplasia JUPAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes3IFQIdentifiersAliasesJUP ARVD12 CTNNG DP3 DPIII PDGB PKGB Plakoglobin junction plakoglobin PGExternal IDsOMIM 173325 MGI 96650 HomoloGene 1680 GeneCards JUPGene location Human Chr Chromosome 17 human 1 Band17q21 2Start41 754 604 bp 1 End41 786 931 bp 1 Gene location Mouse Chr Chromosome 11 mouse 2 Band11 D 11 63 47 cMStart100 259 784 bp 2 End100 288 589 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed inskin of abdomennipplehuman penisvulvabody of tongueoral cavityminor salivary glandsrenal medullaright uterine tubeleft ventricleTop expressed inlipesophaguscorneal stromaskin of backstomachpyloric antrumepithelium of stomachyolk sacskin of abdomencerebellar cortexMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein homodimerization activity transcription coactivator activity structural constituent of cell wall structural molecule activity signal transducer activity protein binding cell adhesive protein binding involved in bundle of His cell Purkinje myocyte communication protein phosphatase binding protein kinase binding alpha catenin binding cell adhesion molecule binding cadherin bindingCellular componentcytoplasm cytosol gamma catenin TCF7L2 complex lateral plasma membrane membrane intercalated disc cell cell junction focal adhesion adherens junction plasma membrane desmosome hemidesmosome cell junction apicolateral plasma membrane protein DNA complex Z disc actin cytoskeleton zonula adherens cytoplasmic side of plasma membrane catenin complex fascia adherens cytoskeleton intermediate filament extracellular exosome nucleus extracellular matrix cornified envelope extracellular region specific granule lumen ficolin 1 rich granule lumenBiological processadherens junction assembly protein heterooligomerization positive regulation of canonical Wnt signaling pathway positive regulation of DNA binding transcription factor activity bundle of His cell Purkinje myocyte adhesion involved in cell communication endothelial cell cell adhesion cellular response to indole 3 methanol desmosome assembly cell adhesion regulation of cell population proliferation detection of mechanical stimulus positive regulation of protein import into nucleus adherens junction organization regulation of heart rate by cardiac conduction cell migration regulation of ventricular cardiac muscle cell action potential skin development signal transduction keratinization neutrophil degranulation cornification protein localization to plasma membrane cell cell adhesion positive regulation of cell matrix adhesion negative regulation of blood vessel endothelial cell migration positive regulation of angiogenesis positive regulation of transcription by RNA polymerase IISources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez372816480EnsemblENSG00000173801ENSMUSG00000001552UniProtP14923Q02257RefSeq mRNA NM 002230NM 021991NM 001352773NM 001352774NM 001352775NM 001352776NM 001352777NM 010593RefSeq protein NP 002221NP 068831NP 001339702NP 001339703NP 001339704NP 001339705NP 001339706NP 034723Location UCSC Chr 17 41 75 41 79 MbChr 11 100 26 100 29 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Structure 2 Function 3 Clinical significance 4 Interactions 5 See also 6 References 7 Further reading 8 External linksStructure editHuman plakoglobin is 81 7 kDa in molecular weight and 745 amino acids long 6 The JUP gene contains 13 exons spanning 17 kb on chromosome 17q21 7 Plakoglobin is a member of the catenin family since it contains a distinct repeating amino acid motif called the armadillo repeat 5 Plakoglobin is highly similar to b catenin both have 12 armadillo repeats as well as N terminal and C terminal globular domains of unknown structure 8 Plakoglobin was originally identified as a component of desmosomes where it can bind to the cadherin family member desmoglein I Plakoglobin also associates with classical cadherins such as E cadherin in that context it was called gamma catenin Plakoglobin forms distinct complexes with cadherins and desmosomal cadherins Function editPlakoglobin is a major cytoplasmic component of both desmosomes and adherens junctions and is the only known constituent common to submembranous plaques in both of these structures 9 which are located at the intercalated disc ICD of cardiomyocytes Plakoglobin links cadherins to the actin cytoskeleton Plakoglobin binds to conserved regions of desmoglein and desmocollin at intracellular catenin binding sites to assemble desmosomes 10 11 Plakoglobin is essential for normal development of intercalated discs and stability of cardiac muscle Transgenic mice homozygous for a null mutation of the JUP gene die around embryonic day 12 from substantial defects in adherens junctions and a lack of functional desmosomes in the heart 12 13 Further studies showed that cardiac fibers obtained from JUP null embryonic mice had decreased passive compliance albeit normal attachment of sarcomeres to adherens junctions 14 In additional studies an inducible cardiac specific plakoglobin knockout mice were generated Transgenic mice displayed a similar phenotype as arrhythmogenic right ventricular cardiomyopathy patients with loss of cardiomyocytes fibrosis and cardiac dysfunction as well as alterations in desmosome protein content and gap junction remodeling Hearts also exhibited increases in b catenin signaling 15 16 Further investigations on the role of b catenin and plakoglobin in the heart generated a double knockout of these two proteins Mice exhibited cardiomyopathy fibrosis conduction abnormalities and sudden cardiac death presumably via spontaneous lethal ventricular arrhythmias Mice also showed a decrease in gap junction structures at intercalated discs 17 Intracellular plakoglobin expression is controlled by Wnt signaling and ubiquitin proteasome dependent degradation Phosphorylation of N terminal Serines by a destruction complex composed of glycogen synthase kinase 3b GSK3b and scaffold proteins adenomatous polyposis coli APC and axin targets plakoglobin for degradation 18 19 20 31 33 The phosphorylated motif is recognized by b TrCP a ubiquitin ligase that targets plakoglobin 26S proteasome dependent degradation 21 Plakoglobin is also O glycosylated near its N terminal destruction box Clinical significance editMutation of the JUP gene encoding plakoglobin has been implicated as one of the causes of the cardiomyopathy known as arrhythmogenic right ventricular dysplasia ARVD or arrhythmogenic right ventricular cardiomyopathy mutations in JUP specifically causes an autosomal recessive form referred to as Naxos disease 22 23 24 This form of was first identified in a small cluster of families on the Greek island of Naxos The phenotype of the Naxos disease variant of ARVD is unique in that it involves the hair and skin as well as the right ventricle Affected individuals have kinky wooly hair there is also palmar and plantar erythema at birth that progresses to keratosis as the palms and soles of the feet are used in crawling and walking 25 26 27 These findings co segregate 100 with the development of ARVD by early adolescence It has become clear that ARVD ARVC is a disease of the cardiac muscle desmosome advances in molecular genetics have illuminated this notion 28 29 30 31 32 33 34 35 36 Studies investigating the role of plakoglobin in disease pathology have found that suppression of desmoplakin expression by siRNA led to the nuclear localization of plakoglobin resulting in a reduction in Wnt signaling via Tcf Lef1 and ensued pathogenesis of ARVC 37 Specifically adipogenic factor expression was induced and cardiac progenitor cells at the epicardium were differentiated to adipocytes 38 Non invasive cardiac screening identified T wave inversion abnormalities in right ventricular wall motion and frequent ventricular extrasystoles as sensitive and specific markers of a JUP mutation 39 Additional studies have shown that immunohistochemical analysis of cardiac muscle desmosomal proteins is also a sensitive and specific diagnostic text for ARVD ARVC 40 Abnormal distribution of plakoglobin due to mutations in genes encoding for Desmoglein 1 and 3 have also been implicated in Pemphigus vulgaris 41 42 Interactions editPlakoglobin has been shown to interact with APC 43 44 CTNNA1 45 46 47 CTNNB1 48 49 CDH1 43 48 50 51 52 CDH2 45 53 CDH3 54 CDH5 55 56 DSG2 57 58 59 DSP 60 61 MUC1 62 PKP2 63 PTPkappa PTPRK 64 PTPrho PTPRT 65 and PDLIM3 66 See also editCatenin List of conditions caused by problems with junctional proteinsReferences edit a b c GRCh38 Ensembl release 89 ENSG00000173801 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000001552 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Entrez Gene JUP junction plakoglobin Protein sequence of human JUP Uniprot ID P14923 Cardiac Organellar Protein Atlas Knowledgebase COPaKB Archived from the original on 24 September 2015 Retrieved 3 July 2015 Whittock NV Eady RA McGrath JA Oct 2000 Genomic organization and amplification of the human plakoglobin gene JUP Experimental Dermatology 9 5 323 6 doi 10 1034 j 1600 0625 2000 009005323 x PMID 11016852 S2CID 12956044 Stokes DL Oct 2007 Desmosomes from a structural perspective Current Opinion in Cell Biology 19 5 565 71 doi 10 1016 j ceb 2007 09 003 PMC 2211412 PMID 17945476 Cowin P Kapprell HP Franke WW Tamkun J Hynes RO Sep 1986 Plakoglobin a protein common to different kinds of intercellular adhering junctions Cell 46 7 1063 73 doi 10 1016 0092 8674 86 90706 3 PMID 3530498 S2CID 45332970 Witcher LL Collins R Puttagunta S Mechanic SE Munson M Gumbiner B Cowin P May 1996 Desmosomal cadherin binding domains of plakoglobin The Journal of Biological Chemistry 271 18 10904 9 doi 10 1074 jbc 271 18 10904 PMID 8631907 Troyanovsky RB Chitaev NA Troyanovsky SM Dec 1996 Cadherin binding sites of plakoglobin localization specificity and role in targeting to adhering junctions Journal of Cell Science 109 13 3069 78 doi 10 1242 jcs 109 13 3069 PMID 9004041 Ruiz P Brinkmann V Ledermann B Behrend M Grund C Thalhammer C Vogel F Birchmeier C Gunthert U Franke WW Birchmeier W Oct 1996 Targeted mutation of plakoglobin in mice reveals essential functions of desmosomes in the 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Shou W Dec 2011 Restrictive loss of plakoglobin in cardiomyocytes leads to arrhythmogenic cardiomyopathy Human Molecular Genetics 20 23 4582 96 doi 10 1093 hmg ddr392 PMC 3209829 PMID 21880664 Swope D Cheng L Gao E Li J Radice GL Mar 2012 Loss of cadherin binding proteins b catenin and plakoglobin in the heart leads to gap junction remodeling and arrhythmogenesis Molecular and Cellular Biology 32 6 1056 67 doi 10 1128 MCB 06188 11 PMC 3295003 PMID 22252313 Kodama S Ikeda S Asahara T Kishida M Kikuchi A Sep 1999 Axin directly interacts with plakoglobin and regulates its stability The Journal of Biological Chemistry 274 39 27682 8 doi 10 1074 jbc 274 39 27682 PMID 10488109 Rubinfeld B Souza B Albert I Munemitsu S Polakis P Mar 1995 The APC protein and E cadherin form similar but independent complexes with alpha catenin beta catenin and plakoglobin The Journal of Biological Chemistry 270 10 5549 55 doi 10 1074 jbc 270 10 5549 PMID 7890674 Kikuchi A Feb 2000 Regulation of beta catenin 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VE cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions a pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions Journal of Cell Science 111 20 3045 57 doi 10 1242 jcs 111 20 3045 PMID 9739078 Kowalczyk AP Bornslaeger EA Borgwardt JE Palka HL Dhaliwal AS Corcoran CM Denning MF Green KJ Nov 1997 The amino terminal domain of desmoplakin binds to plakoglobin and clusters desmosomal cadherin plakoglobin complexes The Journal of Cell Biology 139 3 773 84 doi 10 1083 jcb 139 3 773 PMC 2141713 PMID 9348293 Li Y Yu WH Ren J Chen W Huang L Kharbanda S Loda M Kufe D Aug 2003 Heregulin targets gamma catenin to the nucleolus by a mechanism dependent on the DF3 MUC1 oncoprotein Molecular Cancer Research 1 10 765 75 PMID 12939402 Chen X Bonne S Hatzfeld M van Roy F Green KJ Mar 2002 Protein binding and functional characterization of plakophilin 2 Evidence for its diverse roles in desmosomes and beta catenin signaling The Journal of Biological Chemistry 277 12 10512 22 doi 10 1074 jbc M108765200 PMID 11790773 Fuchs M Muller T Lerch MM Ullrich A Jul 1996 Association of human protein tyrosine phosphatase kappa with members of the armadillo family The Journal of Biological Chemistry 271 28 16712 9 doi 10 1074 jbc 271 28 16712 PMID 8663237 Besco JA Hooft van Huijsduijnen R Frostholm A Rotter A Oct 2006 Intracellular substrates of brain enriched receptor protein tyrosine phosphatase rho RPTPrho PTPRT Brain Research 1116 1 50 7 doi 10 1016 j brainres 2006 07 122 PMID 16973135 S2CID 23343123 Pashmforoush M Pomies P Peterson KL Kubalak S Ross J Hefti A Aebi U Beckerle MC Chien KR May 2001 Adult mice deficient in actinin associated LIM domain protein reveal a developmental pathway for right ventricular cardiomyopathy Nature Medicine 7 5 591 7 doi 10 1038 87920 PMID 11329061 S2CID 1781328 Further reading editCowin P Kapprell HP Franke WW Tamkun J Hynes RO Sep 1986 Plakoglobin a protein common to different kinds of intercellular adhering junctions Cell 46 7 1063 73 doi 10 1016 0092 8674 86 90706 3 PMID 3530498 S2CID 45332970 Franke WW Goldschmidt MD Zimbelmann R Mueller HM Schiller DL Cowin P Jun 1989 Molecular cloning and amino acid sequence of human plakoglobin the common junctional plaque protein Proceedings of the National Academy of Sciences of the United States of America 86 11 4027 31 Bibcode 1989PNAS 86 4027F doi 10 1073 pnas 86 11 4027 PMC 287381 PMID 2726765 Mathur M Goodwin L Cowin P May 1994 Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin The Journal of Biological Chemistry 269 19 14075 80 doi 10 1016 S0021 9258 17 36756 X PMID 8188687 Beavon IR Aug 2000 The E cadherin catenin complex in tumour metastasis structure function and regulation European Journal of Cancer 36 13 Spec No 1607 20 doi 10 1016 S0959 8049 00 00158 1 PMID 10959047 Wilson PD Apr 2001 Polycystin new aspects of structure function and regulation Journal of the American Society of Nephrology 12 4 834 45 doi 10 1681 ASN V124834 PMID 11274246 Protonotarios NI Tsatsopoulou AA Gatzoulis KA Feb 2002 Arrhythmogenic right ventricular cardiomyopathy caused by a deletion in plakoglobin Naxos disease Cardiac Electrophysiology Review 6 1 2 72 80 doi 10 1023 A 1017943323473 PMID 11984022 Knudsen KA Wheelock MJ Aug 1992 Plakoglobin or an 83 kD homologue distinct from beta catenin interacts with E cadherin and N cadherin The Journal of Cell Biology 118 3 671 9 doi 10 1083 jcb 118 3 671 PMC 2289540 PMID 1639850 Arnemann J Spurr NK Wheeler GN Parker AE Buxton RS Jul 1991 Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction desmoglein DGI DSG desmocollins DGII III DSC desmoplakins DPI II DSP and plakoglobin DPIII JUP Genomics 10 3 640 5 doi 10 1016 0888 7543 91 90446 L PMID 1889810 Kinch MS Clark GJ Der CJ Burridge K Jul 1995 Tyrosine phosphorylation regulates the adhesions of ras transformed breast epithelia The Journal of Cell Biology 130 2 461 71 doi 10 1083 jcb 130 2 461 PMC 2199929 PMID 7542250 Aberle H Bierkamp C Torchard D Serova O Wagner T Natt E Wirsching J Heidkamper C Montagna M Lynch HT Jul 1995 The human plakoglobin gene localizes on chromosome 17q21 and is subjected to loss of heterozygosity in breast and ovarian cancers Proceedings of the National Academy of Sciences of the United States of America 92 14 6384 8 Bibcode 1995PNAS 92 6384A doi 10 1073 pnas 92 14 6384 PMC 41522 PMID 7604000 Sacco PA McGranahan TM Wheelock MJ Johnson KR Aug 1995 Identification of plakoglobin domains required for association with N cadherin and alpha catenin The Journal of Biological Chemistry 270 34 20201 6 doi 10 1074 jbc 270 34 20201 PMID 7650039 Daniel JM Reynolds AB Sep 1995 The tyrosine kinase substrate p120cas binds directly to E cadherin but not to the adenomatous polyposis coli protein or alpha catenin Molecular and Cellular Biology 15 9 4819 24 doi 10 1128 mcb 15 9 4819 PMC 230726 PMID 7651399 Kanai Y Ochiai A Shibata T Oyama T Ushijima S Akimoto S Hirohashi S Mar 1995 c erbB 2 gene product directly associates with beta catenin and plakoglobin Biochemical and Biophysical Research Communications 208 3 1067 72 doi 10 1006 bbrc 1995 1443 PMID 7702605 Roh JY Stanley JR May 1995 Plakoglobin binding by human Dsg3 pemphigus vulgaris antigen in keratinocytes requires the cadherin like intracytoplasmic segment The Journal of Investigative Dermatology 104 5 720 4 doi 10 1111 1523 1747 ep12606963 PMID 7738346 Shibamoto S Hayakawa M Takeuchi K Hori T Miyazawa K Kitamura N Johnson KR Wheelock MJ Matsuyoshi N Takeichi M Mar 1995 Association of p120 a tyrosine kinase substrate with E cadherin catenin complexes The Journal of Cell Biology 128 5 949 57 doi 10 1083 jcb 128 5 949 PMC 2120395 PMID 7876318 Rubinfeld B Souza B Albert I Munemitsu S Polakis P Mar 1995 The APC protein and E cadherin form similar but independent complexes with alpha catenin beta catenin and plakoglobin The Journal of Biological Chemistry 270 10 5549 55 doi 10 1074 jbc 270 10 5549 PMID 7890674 Troyanovsky SM Troyanovsky RB Eshkind LG Leube RE Franke WW Nov 1994 Identification of amino acid sequence motifs in desmocollin a desmosomal glycoprotein that are required for plakoglobin binding and plaque formation Proceedings of the National Academy of Sciences of the United States of America 91 23 10790 4 Bibcode 1994PNAS 9110790T doi 10 1073 pnas 91 23 10790 PMC 45111 PMID 7971964 Shibata T Gotoh M Ochiai A Hirohashi S Aug 1994 Association of plakoglobin with APC a tumor suppressor gene product and its regulation by tyrosine phosphorylation Biochemical and Biophysical Research Communications 203 1 519 22 doi 10 1006 bbrc 1994 2213 PMID 8074697 Hinck L Nathke IS Papkoff J Nelson WJ Jun 1994 Dynamics of cadherin catenin complex formation novel protein interactions and pathways of complex assembly The Journal of Cell Biology 125 6 1327 40 doi 10 1083 jcb 125 6 1327 PMC 2290923 PMID 8207061 Arnemann J Sullivan KH Magee AI King IA Buxton RS Mar 1993 Stratification related expression of isoforms of the desmosomal cadherins in human epidermis Journal of Cell Science 104 3 741 50 doi 10 1242 jcs 104 3 741 PMID 8314871 Ozawa M Nuruki K Toyoyama H Ohi Y Oct 1995 Cloning of an alternative form of plakoglobin gamma catenin lacking the fourth armadillo repeat Journal of Biochemistry 118 4 836 40 doi 10 1093 oxfordjournals jbchem a124988 PMID 8576101 Fuchs M Muller T Lerch MM Ullrich A Jul 1996 Association of human protein tyrosine phosphatase kappa with members of the armadillo family The Journal of Biological Chemistry 271 28 16712 9 doi 10 1074 jbc 271 28 16712 PMID 8663237 External links editGeneReviews NCBI NIH UW entry on Arrhythmogenic Right Ventricular Dysplasia Cardiomyopathy Autosomal Dominant OMIM entries on Arrhythmogenic Right Ventricular Dysplasia Cardiomyopathy Autosomal Dominant gamma Catenin at the U S National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title Plakoglobin amp oldid 1217948887, wikipedia, wiki, book, books, library,

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