A Drosophila homolog of cadherin associated with armadillo and essential for embryonic cell-cell adhesion

Dev Biol. 1994 Oct;165(2):716-26. doi: 10.1006/dbio.1994.1287.


We have identified a Drosophila homolog of vertebrate classic cadherins. A monoclonal antibody to Drosophila alpha-catenin (D alpha-catenin) copurifies a 150-kDa glycoprotein (gp150) along with the alpha-catenin. To further characterize this protein, we generated monoclonal antibodies to gp150 and isolated its cDNAs using the antibodies. Predicted sequences of the encoded product revealed that it is a transmembrane protein with similarity to vertebrate classic cadherins, and so we designated this molecule DE-cadherin. The extracellular domain has six cadherin-specific repeats, although the first repeat seems to be cleaved off upon maturation, and the cytoplasmic domain shows significant identity to that of vertebrate classic cadherins. DE-cadherin is distinguishable from its vertebrate counterparts by a large insertion with local sequence similarity to Fat, laminin A chain, Slit, and neurexin I at the proximal region of the extracellular domain. Despite such differences, DE-cadherin is functionally similar to vertebrate classic cadherins. For example, it is associated with alpha-catenin and beta-catenin (Armadillo), and protected from trypsin digestion only in the presence of Ca2+, as is the case for many of classic cadherins. Transfection of S2 cells with the DE-cadherin cDNA enhances their Ca(2+)-dependent cell aggregation. Antibodies to this molecule inhibited aggregation of not only the transfectants but also early embryonic cells. DE-cadherin is concentrated at the apical poles of epithelial cell-cell junctions. All these results suggest that DE-cadherin is a homolog of vertebrate classic cadherins and that the vertebrate and invertebrate share common mechanisms for regulation of cell-cell adhesion.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Armadillo Domain Proteins
  • Cadherins / chemistry*
  • Cell Adhesion
  • Cell Aggregation
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Drosophila Proteins*
  • Drosophila melanogaster / chemistry*
  • Drosophila melanogaster / embryology
  • Glycoproteins / chemistry
  • Glycoproteins / genetics
  • Molecular Sequence Data
  • Multigene Family
  • Proteins / metabolism
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Trans-Activators*
  • Transcription Factors


  • ARM protein, Drosophila
  • Armadillo Domain Proteins
  • Cadherins
  • DNA, Complementary
  • Drosophila Proteins
  • Glycoproteins
  • Proteins
  • Trans-Activators
  • Transcription Factors

Associated data

  • GENBANK/D28749