Abstract
Arrestin is supposed to be involved in uncoupling receptor-mediated second messenger cascades. Clones encoding proteins homologous to arrestin have been isolated from antennal cDNA libraries of Locusta migratoria and Heliothis virescens. Based on the size and several characteristic motifs, the two proteins are considered as members of different arrestin subfamilies. One of the subtypes, which has also been found in Drosophila, lacks the regulatory acidic C-terminal. The putative site of interaction with phosphorylated receptors, a cationic region in the primary structure, is conserved in all identified arrestins from locust to human.
