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PMID: 1664548 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

G-protein-coupled receptor kinases.

Trends in biochemical sciences ·Vol. 16 ·No. 10 ·1991-10-00 ·Pages 387-91

Palczewski K, Benovic JL

Abstract

Rhodopsin kinase and the beta-adrenergic receptor kinase (beta ARK) catalyse the phosphorylation of the activated forms of the G-protein-coupled receptors, rhodopsin and the beta 2-adrenergic receptor (beta 2AR), respectively. The interaction between receptor and kinase is independent of second messengers and appears to involve a multipoint attachment of kinase and substrate with the specificity being restricted by both the primary amino acid sequence and conformation of the substrate. Kinetic, functional and sequence information reveals that rhodopsin kinase and beta ARK are closely related, suggesting they may be members of a family of G-protein-coupled receptor kinases.

MeSH Terms
Animals Cyclic AMP-Dependent Protein Kinases Eye Proteins G-Protein-Coupled Receptor Kinase 1 GTP-Binding Proteins/physiology Humans Phosphorylation Protein Kinases/physiology Receptors, Adrenergic, beta/metabolism Rhodopsin/metabolism beta-Adrenergic Receptor Kinases
Chemicals
Eye Proteins Receptors, Adrenergic, beta Rhodopsin Protein Kinases Cyclic AMP-Dependent Protein Kinases G-Protein-Coupled Receptor Kinase 1 GRK1 protein, human beta-Adrenergic Receptor Kinases GTP-Binding Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Palczewski K
Dow Neurological Sciences Institute, Good Samaritan Hospital and Medical Center, Portland, OR 97209.
Benovic J L
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1991-10-00
Pages
387-91
Language
English
Region
England
NLM ID
7610674
Subset
IM
Grants
NEI NIH HHS · EY08061 · United States
NIGMS NIH HHS · GM44944 · United States
NHLBI NIH HHS · HL45964 · United States
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