The AF-6 homolog Canoe acts as a Rap1 effector during dorsal closure of the Drosophila embryo

Boettner, B., Harjes, P., Ishimaru, S., Heke, M., Fan, H. Q., Qin, Y., Van Aelst, L., Gaul, U. (September 2003) The AF-6 homolog Canoe acts as a Rap1 effector during dorsal closure of the Drosophila embryo. Genetics, 165 (1). pp. 159-169. ISSN 0016-6731

URL: http://www.ncbi.nlm.nih.gov/pubmed/14504224

Abstract

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.

Item Type: Paper
Uncontrolled Keywords: GTPASE-ACTIVATING PROTEIN CELL-ADHESION MAP KINASE RAS BINDING MORPHOGENESIS RECEPTOR GENE SUBFAMILY REGULATOR
Subjects: organism description > animal > insect > Drosophila
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > GTPase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Van Aelst lab
Depositing User: Matt Covey
Date: September 2003
Date Deposited: 01 Apr 2013 19:39
Last Modified: 01 Apr 2013 19:39
PMCID: PMC1462758
Related URLs:
URI: http://repository.cshl.edu/id/eprint/27985

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