Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants.

ABSTRACT: Arrestins constitute a family of small cytoplasmic proteins that mediate deactivation of G-protein-coupled receptors (GPCRs) and are known to be essential for cascade inactivation and receptor desensitization. Alternative splicing produces an array of arrestin gene products that have widely different specificities for their cognate receptors in vitro, but the differential functions of these splice variants in vivo are essentially unknown. Bovine rod photoreceptors express two splice variants of visual arrestin (p44 and p48) that display different affinities for the GPCR rhodopsin. To determine the functions of these splice variants in intact cells, we expressed a transgene encoding either a truncated form of murine arrestin (mArr(1-369), or m44) or the long (p48) isoform in mouse rods lack

SUBMITTER: Burns ME 

PROVIDER: S-EPMC6675359 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature