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PMID: 1656454 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 19 ·1991-10-01 ·Pages 8715-9

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

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Blotting, Northern Cattle Cloning, Molecular Cyclic AMP-Dependent Protein Kinases Eye Proteins G-Protein-Coupled Receptor Kinase 1 Gene Expression Molecular Sequence Data Oligonucleotides/chemistry Phylogeny Polymerase Chain Reaction Protein Kinases/chemistry RNA, Messenger/genetics Receptors, Adrenergic, beta/metabolism Restriction Mapping Rhodopsin/metabolism Sequence Alignment Transfection beta-Adrenergic Receptor Kinases
Chemicals
Eye Proteins Oligonucleotides RNA, Messenger Receptors, Adrenergic, beta Rhodopsin Protein Kinases Cyclic AMP-Dependent Protein Kinases G-Protein-Coupled Receptor Kinase 1 beta-Adrenergic Receptor Kinases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Lorenz W
Howard Hughes Medical Institute, Department of Biochemistry, Duke University Medical Center, Durham, NC 27710.
Inglese J
Palczewski K
Onorato J J
Caron M G
Lefkowitz R J
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.19.8715
Published
1991-10-01
Pages
8715-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC52580
Subset
IM
Grants
NEI NIH HHS · EY0806 · United States
NHLBI NIH HHS · HL16037 · United States
Databases
GENBANK
M73836, S57442, S57444, S57448, S57457, S57504, S57506, S57596, S58152, X59603
External Links
PubMed source DOI: 10.1073/pnas.88.19.8715 PMC Full Text View journal details
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