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Published online
doi:10.1083/jcb.200904001
The Journal of Cell Biology, Vol. 186, No. 1, 57-73
The Rockefeller University Press, 0021-9525 $30.00
© Sawyer et al.
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Article

The Drosophila afadin homologue Canoe regulates linkage of the actin cytoskeleton to adherens junctions during apical constriction



Jessica K. Sawyer1, Nathan J. Harris1, Kevin C. Slep1, Ulrike Gaul3, and Mark Peifer1,2

1 Department of Biology and 2 Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599
3 Laboratory of Developmental Neurogenetics, The Rockefeller University, New York, NY 10065

Correspondence to Mark Peifer: peifer{at}unc.edu

Cadherin-based adherens junctions (AJs) mediate cell adhesion and regulate cell shape change. The nectin–afadin complex also localizes to AJs and links to the cytoskeleton. Mammalian afadin has been suggested to be essential for adhesion and polarity establishment, but its mechanism of action is unclear. In contrast, Drosophila melanogaster’s afadin homologue Canoe (Cno) has suggested roles in signal transduction during morphogenesis. We completely removed Cno from embryos, testing these hypotheses. Surprisingly, Cno is not essential for AJ assembly or for AJ maintenance in many tissues. However, morphogenesis is impaired from the start. Apical constriction of mesodermal cells initiates but is not completed. The actomyosin cytoskeleton disconnects from AJs, uncoupling actomyosin constriction and cell shape change. Cno has multiple direct interactions with AJ proteins, but is not a core part of the cadherin–catenin complex. Instead, Cno localizes to AJs by a Rap1- and actin-dependent mechanism. These data suggest that Cno regulates linkage between AJs and the actin cytoskeleton during morphogenesis.

Abbreviations used in this paper: {alpha}cat, {alpha}-catenin; AJ, adherens junction; Arm, Armadillo; Baz, Bazooka; Cno, Canoe; Ecad, E-cadherin; Ed, Echinoid; moe-GFP, moesin-GFP; MZ, maternal and zygotic; Pyd, Polychaetoid; RA, Ras association; ZO-1, zona occludens-1.

© 2009 Sawyer et al.
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