Multiple isoelectric variants of flightin in Drosophila stretch-activated muscles are generated by temporally regulated phosphorylations

Abstract

Drosophila stretch-activated flight muscles contain flightin, a novel myofibrillar protein that interacts with myosin filaments. We have identified eleven flightin isoelectric variants that can be subdivided into phosphorylated and non-phosphorylated subclasses. Flight muscles of late pupal stage P15, at which time myofibrillogenesis has been completed but the muscle has yet to be used, contain primarily non-phosphorylated variants. A dramatic increase in flightin phosphorylation occurs subsequent to eclosion. As the young adult matures, increasingly phosphorylated variants are generated following a precise ontogenetic progression. Adults 5-6 h old and older contain the entire set of flightin isoelectric variants. All nine phosphovariants remain metabolically active throughout adult life as evidenced by their ability to incorporate radioactive phosphate in older adults. Our results suggest the possibility that all nine phosphorylated variants originate from a single precursor by sequential phosphorylation. Phosphorylation of flightin may thus serve both structural and regulatory functional roles.