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The Drosophila embryonic salivary gland is formed by the invagination and collective migration of cells. Here, we report on a novel developmental role for receptor-type guanylyl cyclase at 76C, Gyc76C, in morphogenesis of the salivary gland. We demonstrate that Gyc76C and downstream cGMP-dependent protein kinase 1 (DG1) function in the gland and surrounding mesoderm to control invagination, collective migration and lumen shape. Loss of gyc76C resulted in glands that failed to invaginate, complete posterior migration and had branched lumens. Salivary gland migration defects of gyc76C mutant embryos were rescued by expression of wild-type gyc76C specifically in the gland or surrounding mesoderm, whereas invagination defects were rescued primarily by expression in the gland. In migrating salivary glands of gyc76C mutant embryos, integrin subunits localized normally to gland-mesoderm contact sites but talin localization in the surrounding circular visceral mesoderm and fat body was altered. The extracellular matrix protein, laminin, also failed to accumulate around the migrating salivary gland of gyc76C mutant embryos, and gyc76C and laminin genetically interacted in gland migration. Our studies suggest that gyc76C controls salivary gland invagination, collective migration and lumen shape, in part by regulating the localization of talin and the laminin matrix.

Receptor guanylyl cyclase Gyc76C is required for invagination, collective migration and lumen shape in the Drosophila embryonic salivary gland