The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase.

W Lorenz, J Inglese, K Palczewski… - Proceedings of the …, 1991 - National Acad Sciences
W Lorenz, J Inglese, K Palczewski, JJ Onorato, MG Caron, RJ Lefkowitz
Proceedings of the National Academy of Sciences, 1991National Acad Sciences
Light-dependent deactivation of rhodopsin as well as homologous desensitization of beta-
adrenergic receptors involves receptor phosphorylation that is mediated by the highly
specific protein kinases rhodopsin kinase (RK) and beta-adrenergic receptor kinase (beta
ARK), respectively. We report here the cloning of a complementary DNA for RK. The
deduced amino acid sequence shows a high degree of homology to beta ARK. In a
phylogenetic tree constructed by comparing the catalytic domains of several protein kinases …
Light-dependent deactivation of rhodopsin as well as homologous desensitization of beta-adrenergic receptors involves receptor phosphorylation that is mediated by the highly specific protein kinases rhodopsin kinase (RK) and beta-adrenergic receptor kinase (beta ARK), respectively. We report here the cloning of a complementary DNA for RK. The deduced amino acid sequence shows a high degree of homology to beta ARK. In a phylogenetic tree constructed by comparing the catalytic domains of several protein kinases, RK and beta ARK are located on a branch close to, but separate from the cyclic nucleotide-dependent protein kinase and protein kinase C subfamilies. From the common structural features we conclude that both RK and beta ARK are members of a newly delineated gene family of guanine nucleotide-binding protein (G protein)-coupled receptor kinases that may function in diverse pathways to regulate the function of such receptors.
National Acad Sciences