Open Access Articles- Top Results for Plakoglobin


External IDsOMIM173325 MGI96650 HomoloGene1680 GeneCards: JUP Gene
RNA expression pattern
File:PBB GE JUP 201015 s at tn.png
More reference expression data
RefSeq (mRNA)NM_002230NM_010593
RefSeq (protein)NP_002221NP_034723
Location (UCSC)Chr 17:
39.78 – 39.94 Mb
Chr 11:
100.37 – 100.4 Mb
PubMed search[1][2]

Junction plakoglobin, also known as gamma-catenin or JUP, is a protein that in humans is encoded by the JUP gene.[1] It is a member of the catenin protein family and homologous to β-catenin.


This gene encodes a major cytoplasmic protein that is the only known constituent common to submembranous plaques of both desmosomes and intermediate junctions. This protein forms distinct complexes with cadherins and desmosomal cadherins and is a member of the catenin family, since it contains a distinct repeating amino acid motif called the armadillo repeat.[1]

Plakoglobin (gamma-catenin) 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 is O-glycosylated near its N-terminal destruction box.

Clinical significance

Mutation of the gene encoding plakoglobin has been implicated as one of the causes of the cardiomyopathy known as arrhythmogenic right ventricular dysplasia (ARVD).[2] The form of ARVD in which a mutated form of plakoglobin is present was first identified in a small cluster of families on the Greek island of Naxos. This form of the disorder is autosomal recessive. The phenotype of the Naxos variant of ARVD is unique in that it involves the hair and skin as well as the right ventricle. Affected individuals have wooly, kinky 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. These findings co-segregate 100% with the development of ARVD by early adolescence.

It is also implicated in Pemphigus vulgaris along with genes encoding for Desmoglein 1 and 3.


Plakoglobin has been shown to interact with:

See also


  1. ^ a b "Entrez Gene: JUP junction plakoglobin". 
  2. ^ Garcia-Gras E, Lombardi R, Giocondo MJ, Willerson JT, Schneider MD, Khoury DS, Marian AJ (July 2006). "Suppression of canonical Wnt/β-catenin signaling by nuclear plakoglobin recapitulates phenotype of arrhythmogenic right ventricular cardiomyopathy". J. Clin. Invest. 116 (7): 2012–21. PMC 1483165. PMID 16823493. doi:10.1172/JCI27751. 
  3. ^ a b Shibata T, Gotoh M, Ochiai A, Hirohashi S (August 1994). "Association of plakoglobin with APC, a tumor suppressor gene product, and its regulation by tyrosine phosphorylation". Biochem. Biophys. Res. Commun. 203 (1): 519–22. PMID 8074697. doi:10.1006/bbrc.1994.2213. 
  4. ^ Daniel JM, Reynolds A B (September 1995). "The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin". Mol. Cell. Biol. 15 (9): 4819–24. PMC 230726. PMID 7651399. 
  5. ^ a b Sacco PA, McGranahan T M, Wheelock M J, Johnson K R (August 1995). "Identification of plakoglobin domains required for association with N-cadherin and alpha-catenin". J. Biol. Chem. 270 (34): 20201–6. PMID 7650039. doi:10.1074/jbc.270.34.20201. 
  6. ^ Roe S, Koslov E R, Rimm D L (June 1998). "A mutation in alpha-catenin disrupts adhesion in clone A cells without perturbing its actin and beta-catenin binding activity". Cell Adhes. Commun. 5 (4): 283–96. PMID 9762469. doi:10.3109/15419069809040298. 
  7. ^ Obama H, Ozawa M (April 1997). "Identification of the domain of alpha-catenin involved in its association with beta-catenin and plakoglobin (gamma-catenin)". J. Biol. Chem. 272 (17): 11017–20. PMID 9110993. doi:10.1074/jbc.272.17.11017. 
  8. ^ a b Hazan RB, Norton L (April 1998). "The epidermal growth factor receptor modulates the interaction of E-cadherin with the actin cytoskeleton". J. Biol. Chem. 273 (15): 9078–84. PMID 9535896. doi:10.1074/jbc.273.15.9078. 
  9. ^ Kucerová D, Sloncová E, Tuhácková Z, Vojtechová M, Sovová V (December 2001). "Expression and interaction of different catenins in colorectal carcinoma cells". Int. J. Mol. Med. 8 (6): 695–8. PMID 11712088. doi:10.3892/ijmm.8.6.695. 
  10. ^ Kinch MS, Clark G J, Der C J, Burridge K (July 1995). "Tyrosine phosphorylation regulates the adhesions of ras-transformed breast epithelia". J. Cell Biol. 130 (2): 461–71. PMC 2199929. PMID 7542250. doi:10.1083/jcb.130.2.461. 
  11. ^ Hinck L, Näthke I S, Papkoff J, Nelson W J (June 1994). "Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly". J. Cell Biol. 125 (6): 1327–40. PMC 2290923. PMID 8207061. doi:10.1083/jcb.125.6.1327. 
  12. ^ Knudsen KA, Wheelock M J (August 1992). "Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin". J. Cell Biol. 118 (3): 671–9. PMC 2289540. PMID 1639850. doi:10.1083/jcb.118.3.671. 
  13. ^ Straub BK, Boda Judit, Kuhn Caecilia, Schnoelzer Martina, Korf Ulrike, Kempf Tore, Spring Herbert, Hatzfeld Mechthild, Franke Werner W (December 2003). "A novel cell-cell junction system: the cortex adhaerens mosaic of lens fiber cells". J. Cell. Sci. 116 (Pt 24): 4985–95. PMID 14625392. doi:10.1242/jcs.00815. 
  14. ^ Klingelhöfer J, Troyanovsky R B, Laur O Y, Troyanovsky S (August 2000). "Amino-terminal domain of classic cadherins determines the specificity of the adhesive interactions". J. Cell. Sci. 113 (16): 2829–36. PMID 10910767. 
  15. ^ Lewalle JM, Bajou K, Desreux J, Mareel M, Dejana E, Noël A, Foidart J M (December 1997). "Alteration of interendothelial adherens junctions following tumor cell-endothelial cell interaction in vitro". Exp. Cell Res. 237 (2): 347–56. PMID 9434630. doi:10.1006/excr.1997.3799. 
  16. ^ Shasby DM, Ries Dana R, Shasby Sandra S, Winter Michael C (June 2002). "Histamine stimulates phosphorylation of adherens junction proteins and alters their link to vimentin". Am. J. Physiol. Lung Cell Mol. Physiol. 282 (6): L1330–8. PMID 12003790. doi:10.1152/ajplung.00329.2001. 
  17. ^ Bannon LJ, Cabrera B L, Stack M S, Green K J (November 2001). "Isoform-specific differences in the size of desmosomal cadherin/catenin complexes". J. Invest. Dermatol. 117 (5): 1302–6. PMID 11710948. doi:10.1046/j.1523-1747.2001.01512.x. 
  18. ^ "The amino- and carboxyl-terminal tails of (beta)-catenin reduce its affinity for desmoglein 2". J. Cell. Sci. 113 (10): 1737–45. May 2000. PMID 10769205. 
  19. ^ Ozawa M, Terada H, Pedraza C (November 1995). "The fourth armadillo repeat of plakoglobin (gamma-catenin) is required for its high affinity binding to the cytoplasmic domains of E-cadherin and desmosomal cadherin Dsg2, and the tumor suppressor APC protein". J. Biochem. 118 (5): 1077–82. PMID 8749329. doi:10.1093/jb/118.5.1077. 
  20. ^ Kowalczyk AP, Navarro P, Dejana E, Bornslaeger E A, Green K J, Kopp D S, Borgwardt J E (October 1998). "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". J. Cell. Sci. 111 (20): 3045–57. PMID 9739078. 
  21. ^ Kowalczyk AP, Bornslaeger E A, Borgwardt J E, Palka H L, Dhaliwal A S, Corcoran C M, Denning M F, Green K J (November 1997). "The Amino-terminal Domain of Desmoplakin Binds to Plakoglobin and Clusters Desmosomal Cadherin–Plakoglobin Complexes". J. Cell Biol. 139 (3): 773–84. PMC 2141713. PMID 9348293. doi:10.1083/jcb.139.3.773. 
  22. ^ Li Y, Yu Wei-Hsuan, Ren Jian, Chen Wen, Huang Lei, Kharbanda Surender, Loda Massimo, Kufe Donald (August 2003). "Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein". Mol. Cancer Res. 1 (10): 765–75. PMID 12939402. 
  23. ^ Chen X, Bonne Stefan, Hatzfeld Mechthild, van Roy Frans, Green Kathleen J (March 2002). "Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta -catenin signaling". J. Biol. Chem. 277 (12): 10512–22. PMID 11790773. doi:10.1074/jbc.M108765200. 
  24. ^ Fuchs M, Müller T, Lerch M M, Ullrich A (July 1996). "Association of human protein-tyrosine phosphatase kappa with members of the armadillo family". J. Biol. Chem. 271 (28): 16712–9. PMID 8663237. doi:10.1074/jbc.271.28.16712. 
  25. ^ Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A (2006). "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT).". Brain Res 1116 (1): 50–7. PMID 16973135. doi:10.1016/j.brainres.2006.07.122. 

Further reading


External links