Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Sprouty was identified in a genetic screen as an inhibitor of Drosophila EGF receptor signaling. The Egfr triggers cell recruitment in the eye, and sprouty- eyes have excess photoreceptors, cone cells, and pigment cells. Sprouty's function is, however, more widespread. We show that it also interacts genetically with the receptor tyrosine kinases Torso and Sevenless, and it was first discovered through its effect on FGF receptor signaling. In contrast to an earlier proposal that Sprouty is extracellular, we show by biochemical analysis that Sprouty is an intracellular protein, associated with the inner surface of the plasma membrane. Sprouty binds to two intracellular components of the Ras pathway, Drk and Gap1. Our results indicate that Sprouty is a widespread inhibitor of Ras pathway signal transduction.


Journal article



Publication Date





655 - 665


Animals, Cells, Cultured, Cysteine, Depression, Chemical, Drosophila Proteins, Drosophila melanogaster, Eye, Eye Abnormalities, Eye Proteins, Insect Proteins, Macromolecular Substances, Membrane Glycoproteins, Membrane Proteins, Morphogenesis, Proteins, Receptor Protein-Tyrosine Kinases, Receptor, Epidermal Growth Factor, Signal Transduction, ras GTPase-Activating Proteins, ras Proteins