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


Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Lorenz, W; Inglese, J; Palczewski, K; Onorato, JJ; Caron, MG; Lefkowitz, RJ

Published Date

  • October 1, 1991

Published In

Volume / Issue

  • 88 / 19

Start / End Page

  • 8715 - 8719

PubMed ID

  • 1656454

Pubmed Central ID

  • 1656454

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.88.19.8715


  • eng

Conference Location

  • United States