Genetics, Vol. 165, 159-169, September 2003, Copyright © 2003

The AF-6 Homolog Canoe Acts as a Rap1 Effector During Dorsal Closure of the Drosophila Embryo

Benjamin Boettnerb, Phoebe Harjesa, Satoshi Ishimarua, Michael Hekea, Hong Qing Fana, Yi Qinb, Linda Van Aelstb, and Ulrike Gaula
a Laboratory of Developmental Neurogenetics, Rockefeller University, New York, New York 10021
b Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724

Corresponding author: Ulrike Gaul, Laboratory of Developmental Neurogenetics, 1230 York Ave., New York, NY 10021., gaul{at}mail.rockefeller.edu (E-mail)

Communicating editor: T. SCHÜPBACH

Rap1 belongs to the highly conserved Ras subfamily of small GTPases. In Drosophila, Rap1 plays a critical role in many different morphogenetic processes, but the molecular mechanisms executing its function are unknown. Here, we demonstrate that Canoe (Cno), the Drosophila homolog of mammalian junctional protein AF-6, acts as an effector of Rap1 in vivo. Cno binds to the activated form of Rap1 in a yeast two-hybrid assay, the two molecules colocalize to the adherens junction, and they display very similar phenotypes in embryonic dorsal closure (DC), a process that relies on the elongation and migration of epithelial cell sheets. Genetic interaction experiments show that Rap1 and Cno act in the same molecular pathway during DC and that the function of both molecules in DC depends on their ability to interact. We further show that Rap1 acts upstream of Cno, but that Rap1, unlike Cno, is not involved in the stimulation of JNK pathway activity, indicating that Cno has both a Rap1-dependent and a Rap1-independent function in the DC process.





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