Abstract
Sprouty proteins act as intracellular inhibitors of receptor tyrosine kinase signaling. Here we show that the mammalian Sprouty2 protein contains an iron-sulfur complex that can exist in an oxidized, reduced, or nitrosylated state. Purified Sprouty2 assembles into large monodisperse spheres containing approximately 24 polypeptides per particle. Biochemical experiments indicate that the charge state of the iron within Sprouty2 particles may be insulated from ambient intracellular redox. These features offer the possibility that Sprouty2 particles are capable of receiving, maintaining, and dissipating electrical charge in a manner formally equivalent to a battery.