Isolation of Drosophila genes encoding G protein-coupled receptor kinases.
- 15 December 1991
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 88 (24) , 11067-11070
- https://doi.org/10.1073/pnas.88.24.11067
Abstract
G protein-coupled receptors are regulated via phosphorylation by a variety of protein kinases. Recently, termination of the active state of two such receptors, the beta-adrenergic receptor and rhodopsin, has been shown to be mediated by agonist- or light-dependent phosphorylation of the receptor by members of a family of protein-serine/threonine kinases (here referred to as G protein-coupled receptor kinases). We now report the isolation of a family of genes encoding a set of Drosophila protein kinases that appear to code for G protein-coupled receptor kinases. These proteins share a high degree of sequence homology with the bovine beta-adrenergic receptor kinase. The presence of a conserved family of G protein-coupled receptor kinases in vertebrates and invertebrates points to the central role of these kinases in signal transduction cascades.Keywords
This publication has 39 references indexed in Scilit:
- Detection of specific sequences among DNA fragments separated by gel electrophoresisPublished by Elsevier ,2006
- Phorbol‐ester‐induced phosphorylation of the β2‐adrenergic receptor decreases its coupling to GsFEBS Letters, 1991
- β-Arrestin: a Protein that Regulates β-adrenergic Receptor FunctionScience, 1990
- Phosphorylation of chick heart muscarinic cholinergic receptors by the .beta.-adrenergic receptor kinaseBiochemistry, 1989
- Structure of the Adrenergic and Related ReceptorsAnnual Review of Neuroscience, 1989
- Rhodopsin kinase: substrate specificity and factors that influence activityBiochemistry, 1988
- Deactivation of Photoactivated Rhodopsin by Rhodopsin-Kinase and ArrestinJournal of Receptor Research, 1987
- Light-dependent phosphorylation of rhodopsin by β-adrenergic receptor kinaseNature, 1986
- Light‐induced binding of 48‐kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsinFEBS Letters, 1984
- Light dependent phosphorylation of rhodopsin by ATPFEBS Letters, 1972