DE-cadherin, a core component of the adherens junction complex modifies subcellular localization of the Drosophila gap junction protein innexin2

• Published in: Cell communication & adhesion Vol. 13; no. 1-2; p. 103
• Main Authors: Bauer, R, Weimbs, A, Lechner, H, Hoch, M
• Format: Journal Article
• Language: English
• Published: England 01.01.2006
• Subjects: Adherens Junctions - chemistry; Adherens Junctions - ultrastructure; Animals; Armadillo Domain Proteins - analysis; Cadherins - physiology; Catenins - chemistry; Catenins - metabolism; Cell Adhesion; Connexins - analysis; Connexins - metabolism; Drosophila; Drosophila Proteins - analysis; Drosophila Proteins - metabolism; Drosophila Proteins - physiology; Epithelium - embryology; Epithelium - metabolism; Gap Junctions - chemistry; Gap Junctions - ultrastructure; Transcription Factors - analysis
• ISSN: 1541-9061; 1543-5180
• DOI: 10.1080/15419060600631839

The Drosophila innexin multigene family of gap junction encoding proteins consists of eight family members whose function in epithelial morphogenesis is mostly unknown. We have recently shown that innexin2 plays a crucial role in the organization of embryonic epithelia. Innexin2 protein accumulates in the epidermis in the apico-lateral membrane domain and colocalizes with core proteins of adherens junctions, such as DE-cadherin and Armadillo, the ss -catenin homolog. Innexin2 localization is altered in both armadillo and DE-cadherin mutants Biochemical interaction studies point to a direct interaction of DE-cadherin and Armadillo with innexin2 suggesting a close link between gap junction and adherens junction biogenesis. We have used the Drosophila Schneider cell tissue culture system to further study the interaction of innexin2 with DE-cadherin. Our results provide evidence that DE-cadherin may be a key component to control trafficking, and localization of Innexin2 to the plasma membrane.