Phosphorylation of endogenous proteins by a cyclic amp-dependent protein kinase in the wing epidermis of Manduca sexta

Abstract

The wing epidermis of Manduca sexta has 8 prominent proteins of molecular weights ranging from 18,000 to 55,000, the in vitro phosphorylation of which is enhanced significantly by cAMP. The level of protein phosphorylation during pupal-adult development can be correlated with the changing hemolymph ecdysteroid titer. These protein substrates are not limited to the wing epidermis, being present in the pupal brain, fat body, prothoracic gland and gut, as well as larval integumented epidermis, muscle and the wing imaginal discs. Most of the phosphoproteins stimulated by cAMP were localized in the microsomal fraction of tissue homogenates. The 31/32 kDa doublet phosphoproteins were further localized to a ribosome enriched microsomal fraction and have properties similar to those of mammalian ribosomal protein S6.