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

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

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

dc.contributor.author	Lorenz, W
dc.contributor.author	Inglese, J
dc.contributor.author	Palczewski, K
dc.contributor.author	Onorato, JJ
dc.contributor.author	Caron, MG
dc.contributor.author	Lefkowitz, RJ
dc.coverage.spatial	United States
dc.date.accessioned	2013-09-10T18:01:23Z
dc.date.issued	1991-10-01
dc.description.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.
dc.identifier	https://www.ncbi.nlm.nih.gov/pubmed/1656454
dc.identifier.issn	0027-8424
dc.identifier.uri	https://hdl.handle.net/10161/7851
dc.language	eng
dc.publisher	Proceedings of the National Academy of Sciences
dc.relation.ispartof	Proc Natl Acad Sci U S A
dc.subject	Amino Acid Sequence
dc.subject	Animals
dc.subject	Base Sequence
dc.subject	Blotting, Northern
dc.subject	Cattle
dc.subject	Cloning, Molecular
dc.subject	Cyclic AMP-Dependent Protein Kinases
dc.subject	Eye Proteins
dc.subject	G-Protein-Coupled Receptor Kinase 1
dc.subject	Gene Expression
dc.subject	Molecular Sequence Data
dc.subject	Oligonucleotides
dc.subject	Phylogeny
dc.subject	Polymerase Chain Reaction
dc.subject	Protein Kinases
dc.subject	RNA, Messenger
dc.subject	Receptors, Adrenergic, beta
dc.subject	Restriction Mapping
dc.subject	Rhodopsin
dc.subject	Sequence Alignment
dc.subject	Transfection
dc.subject	beta-Adrenergic Receptor Kinases
dc.title	The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase.
dc.type	Journal article
duke.contributor.orcid	Lefkowitz, RJ\|0000-0003-1472-7545
pubs.author-url	https://www.ncbi.nlm.nih.gov/pubmed/1656454
pubs.begin-page	8715
pubs.end-page	8719
pubs.issue	19
pubs.organisational-group	Basic Science Departments
pubs.organisational-group	Biochemistry
pubs.organisational-group	Cell Biology
pubs.organisational-group	Chemistry
pubs.organisational-group	Clinical Science Departments
pubs.organisational-group	Duke
pubs.organisational-group	Duke Cancer Institute
pubs.organisational-group	Duke Institute for Brain Sciences
pubs.organisational-group	Institutes and Centers
pubs.organisational-group	Institutes and Provost's Academic Units
pubs.organisational-group	Medicine
pubs.organisational-group	Medicine, Cardiology
pubs.organisational-group	Neurobiology
pubs.organisational-group	Pathology
pubs.organisational-group	School of Medicine
pubs.organisational-group	Trinity College of Arts & Sciences
pubs.organisational-group	University Institutes and Centers
pubs.publication-status	Published
pubs.volume	88

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