ArticleBiology open2013
Receptor guanylyl cyclase Gyc76C is required for invagination, collective migration and lumen shape in the Drosophila embryonic salivary gland.
Article in Biology open, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Anti-diuretic hormone ITP signals via a guanylate cyclase receptor to modulate systemic homeostasis ineLife · 2025Article
- Receptor-Type Guanylyl Cyclase at 76C (Gyc76C) Regulates De Novo Lumen Formation during Drosophila Tracheal Development.PloS one · 2016Article
- Article
- Identification and functional analysis of healing regulators in Drosophila.PLoS genetics · 2015Article
- Building and specializing epithelial tubular organs: the Drosophila salivary gland as a model system for revealing how epithelial organs are specified, form and specialize.Wiley interdisciplinary reviews. Developmental biologyReview
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
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.
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