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Gene Review

jup-b  -  junction plakoglobin

Xenopus laevis

Synonyms: arvd12, ctnng, dp3, dpiii, jup, ...
 
 
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High impact information on Jup

  • The sequence is homologous to mammalian plakoglobin, a protein of desmosomal and zonula adherens cell junctions, and to the plakoglobin homolog in Drosophila melanogaster, the product of the segment polarity gene armadillo [1].
  • As a functional assay for the actin skeleton, we show that wound healing, an actin-based behavior in embryos, is also abrogated by plakoglobin depletion [2].
  • Here, we show that this is due to loss of the cortical actin skeleton after depletion of plakoglobin, whereas the microtubule and cytokeratin skeletons are still present [2].
  • We showed previously that depletion of plakoglobin protein during the egg to gastrula stages caused collapse of embryonic architecture [2].
  • We conclude that in Xenopus, the actin skeleton is a major determinant of cell shape and overall architecture in the early embryo, and that plakoglobin plays an essential role in the assembly, maintenance, or organization of this cortical actin [2].
 

Biological context of Jup

  • We have isolated a cDNA encoding the junctional plaque protein plakoglobin of Xenopus laevis and determined its amino acid sequence [3].
  • However, when plakoglobin is artificially engineered to restrict it to the cytoplasm by fusion with the transmembrane domain of connexin (cnxPg), it efficiently induces a Wnt-like axis duplication phenotype in Xenopus [4].
  • Competition among these proteins for binding sites on plakoglobin may therefore account for the distinct composition of adherens junctions and desmosomes [5].
  • However, beta-catenin continues to be detected at the neurula, tailbud, and tadpole stages when levels of plakoglobin decline [6].
  • Expression of a form of PKG truncated after the 5th ARM repeat produced a milder cell adhesion defect, whereas expression of a polypeptide truncated after the 8th ARM repeat had little apparent effect on cellular adhesion [7].
 

Anatomical context of Jup

  • Identification of plakoglobin in oocytes and early embryos of Xenopus laevis: maternal expression of a gene encoding a junctional plaque protein [3].
  • To test whether simply increasing the level of plakoglobin mimics the effects of exogenous wnts in Xenopus, we injected fertilized eggs with RNA encoding an epitope-tagged form of plakoglobin; this induced both early radial gastrulation and anterior axis duplication [8].
  • These data show that increased plakoglobin levels can, by themselves, generate the intracellular signals involved in the specification of dorsal mesoderm [8].
  • Plakoglobin is a major component of both desmosomes and adherens junctions [5].
  • Prior to the midblastula transition exogenous plakoglobin is cytoplasmic and concentrated in the cortical regions of blastomeres; after the midblastula transition exogenous plakoglobin accumulates in embryonic nuclei [9].
 

Other interactions of Jup

References

  1. A homolog of the armadillo protein in Drosophila (plakoglobin) associated with E-cadherin. McCrea, P.D., Turck, C.W., Gumbiner, B. Science (1991) [Pubmed]
  2. Plakoglobin is required for maintenance of the cortical actin skeleton in early Xenopus embryos and for cdc42-mediated wound healing. Kofron, M., Heasman, J., Lang, S.A., Wylie, C.C. J. Cell Biol. (2002) [Pubmed]
  3. Identification of plakoglobin in oocytes and early embryos of Xenopus laevis: maternal expression of a gene encoding a junctional plaque protein. Fouquet, B., Zimbelmann, R., Franke, W.W. Differentiation (1992) [Pubmed]
  4. Membrane-anchored plakoglobins have multiple mechanisms of action in Wnt signaling. Klymkowsky, M.W., Williams, B.O., Barish, G.D., Varmus, H.E., Vourgourakis, Y.E. Mol. Biol. Cell (1999) [Pubmed]
  5. Desmosomal cadherin binding domains of plakoglobin. Witcher, L.L., Collins, R., Puttagunta, S., Mechanic, S.E., Munson, M., Gumbiner, B., Cowin, P. J. Biol. Chem. (1996) [Pubmed]
  6. The armadillo homologs beta-catenin and plakoglobin are differentially expressed during early development of Xenopus laevis. DeMarais, A.A., Moon, R.T. Dev. Biol. (1992) [Pubmed]
  7. Localizing the adhesive and signaling functions of plakoglobin. Rubenstein, A., Merriam, J., Klymkowsky, M.W. Dev. Genet. (1997) [Pubmed]
  8. Anterior axis duplication in Xenopus induced by the over-expression of the cadherin-binding protein plakoglobin. Karnovsky, A., Klymkowsky, M.W. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  9. Cytoplasmically anchored plakoglobin induces a WNT-like phenotype in Xenopus. Merriam, J.M., Rubenstein, A.B., Klymkowsky, M.W. Dev. Biol. (1997) [Pubmed]
  10. The roles of maternal alpha-catenin and plakoglobin in the early Xenopus embryo. Kofron, M., Spagnuolo, A., Klymkowsky, M., Wylie, C., Heasman, J. Development (1997) [Pubmed]
  11. Misexpression of the catenin p120(ctn)1A perturbs Xenopus gastrulation but does not elicit Wnt-directed axis specification. Paulson, A.F., Fang, X., Ji, H., Reynolds, A.B., McCrea, P.D. Dev. Biol. (1999) [Pubmed]
 
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