Abstract
EGF signaling is a well-known oncogenic pathway in animals. It is also a key developmental pathway regulating terminal and dorsal-ventral patterning along with many other aspects of embryogenesis. In this review, we focus on the diverse roles for the EGF pathway in Drosophila embryogenesis. We review the existing body of evidence concerning EGF signaling in Drosophila embryogenesis focusing on current uncertainties in the field and areas for future study. This review provides a foundation for utilizing the Drosophila model system for research into EGF effects on cancer.
Highlights
Rho-1 is understood to be the primary effector of the EGF response, due to its ability to respond both to positive feedback and to induce EGF signaling in neighboring cells in oogenesis [25]
Cadherin based cell adhesion remains unclear, but a connection was suggested by another study which showed that in the absence of EGF signaling, developing tracheal cells are unable to concentrate filamentous Actin causing a defect in tracheal invagination [69]
EGF often functions in cell growth and proliferation and regulates apoptosis
Summary
The Drosophila homolog of the epidermal growth factor receptor abbreviated as EGFR is known by several names—faint little ball and torpedo—with flb referring to the embryonic phenotype and torpedo referring to an oogenesis defect observed in eggs [1], DER and Ellipse for imaginal disc and adult eye phenotypes [2,3]. Spi is able to rescue vn mutants and modulates its activity to roughly match the activation by vn [10] Overall, these three types of ligands which serve similar functions, allow the EGF pathway to signal in a variety of conditions increasing its accuracy and specificity in effecting cellular changes in response to other developmental events. It is possible that the broad diversity and critical nature of EGF signaling both in development and in a wide range of other biological processes has influenced the development of redundant ligands with subtly differing regulatory mechanism or strength It is possible, especially given the similarity of spi, krn, and grk to TGF-α, and vn’s corresponding dissimilarity, that any of these ligands were co-opted from another function early in evolution, and the original function was later lost, with the ligand taking on a new role as a redundant regulator of the EGF signal. The finding that arg binds to the EGF receptor, not the ligand, and in a manner different from the ligands, is consistent with the idea that several ligands were co-opted from other functions while the inhibitory ligand (of which only one exists) was central to the function of the receptor prior to the evolutionary events where other ligands were co-opted [22]
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