Gap Junction Channel Protein Innexin 2 Is Essential for Epithelial Morphogenesis in the Drosophila Embryo
| Autor: | Corinna Lehmann, Julia Martini, Michael Hoch, Franka Eckardt, Reinhard Bauer |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Embryo
Nonmammalian Gap junction Connexin Gap Junctions Septate junctions Epithelial Cells Cell Biology Innexin Articles Biology Transmembrane protein Connexins Epithelium Transport protein Cell biology Adherens junction Protein Transport Drosophila melanogaster Antibody Specificity Morphogenesis Animals Drosophila Proteins Molecular Biology Drosophila Protein Protein Binding |
| Popis: | Direct communication of neighboring cells by gap junction channels is essential for the development of tissues and organs in the body. Whereas vertebrate gap junctions are composed of members of the connexin family of transmembrane proteins, in invertebrates gap junctions consist of Innexin channel proteins. Innexins display very low sequence homology to connexins. In addition, very little is known about their cellular role during developmental processes. In this report, we examined the function and the distribution of Drosophila Innexin 2 protein in embryonic epithelia. Both loss-of-function and gain-of-function innexin 2 mutants display severe developmental defects due to cell death and a failure of proper epithelial morphogenesis. Furthermore, immunohistochemical analyses using antibodies against the Innexins 1 and 2 indicate that the distribution of Innexin gap junction proteins to specific membrane domains is regulated by tissue specific factors. Finally, biochemical interaction studies together with genetic loss- and gain-of-function experiments provide evidence that Innexin 2 interacts with core proteins of adherens and septate junctions. This is the first study, to our knowledge, of cellular distribution and protein–protein interactions of an Innexin gap junctional channel protein in the developing epithelia of Drosophila. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|