Intercellular communication: the Drosophila innexin multiprotein family of gap junction proteins

Chem Biol. 2005 May;12(5):515-26. doi: 10.1016/j.chembiol.2005.02.013.


Gap junctions belong to the most conserved cellular structures in multicellular organisms, from Hydra to man. They contain tightly packed clusters of hydrophilic membrane channels connecting the cytoplasms of adjacent cells, thus allowing direct communication of cells and tissues through the diffusion of ions, metabolites, and cyclic nucleotides. Recent evidence suggests that gap junctions are constructed by three different families of four transmembrane proteins: the Connexins and the Innexins found in vertebrates and in invertebrates, respectively, and the Innexin-like Pannexins, which were recently discovered in humans. This article focuses on the Drosophila Innexin multiprotein family, which is comprised of eight members. We highlight common structural features and discuss recent findings that suggest close similarities in cellular distribution, function, and regulation of Drosophila Innexins and vertebrate gap junction proteins.

Publication types

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

MeSH terms

  • Adherens Junctions
  • Amino Acid Sequence
  • Animals
  • Connexins / genetics*
  • Drosophila Proteins / genetics*
  • Gap Junctions / genetics*
  • Humans
  • Intercellular Signaling Peptides and Proteins
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Signal Transduction*
  • Structural Homology, Protein
  • Wnt Proteins


  • Connexins
  • Drosophila Proteins
  • Intercellular Signaling Peptides and Proteins
  • Wnt Proteins