beta-Arrestin: a protein that regulates beta-adrenergic receptor
function
M. Lohse, J. Benovic, J. Codina, M. Caron, and R. Lefkowitz. Science, 248 (4962):
1547-50(June 1990)Lohse, M J Benovic, J L Codina, J Caron, M G Lefkowitz, R J DK19318/DK/NIDDK
NIH HHS/United States HL16037/HL/NHLBI NIH HHS/United States Research
Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. United
states Science (New York, N.Y.) Science. 1990 Jun 22;248(4962):1547-50..
Abstract
Homologous or agonist-specific desensitization of beta-adrenergic
receptors is thought to be mediated by a specific kinase, the beta-adrenergic
receptor kinase (beta ARK). However, recent data suggest that a cofactor
is required for this kinase to inhibit receptor function. The complementary
DNA for such a cofactor was cloned and found to encode a 418-amino
acid protein homologous to the retinal protein arrestin. The protein,
termed beta-arrestin, was expressed and partially purified. It inhibited
the signaling function of beta ARK-phosphorylated beta-adrenergic
receptors by more than 75 percent, but not that of rhodopsin. It
is proposed that beta-arrestin in concert with beta ARK effects homologous
desensitization of beta-adrenergic receptors.
Lohse, M J Benovic, J L Codina, J Caron, M G Lefkowitz, R J DK19318/DK/NIDDK
NIH HHS/United States HL16037/HL/NHLBI NIH HHS/United States Research
Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. United
states Science (New York, N.Y.) Science. 1990 Jun 22;248(4962):1547-50.
%0 Journal Article
%1 Lohse1990a
%A Lohse, M. J.
%A Benovic, J. L.
%A Codina, J.
%A Caron, M. G.
%A Lefkowitz, R. J.
%D 1990
%J Science
%K & *Cyclic AMP-Dependent Acid Amino Animals Antigens/*genetics/isolation Arrestin Blotting, Chromatography, Cloning, DNA/genetics Data Exchange Expression Eye Gene Inhibitors/*pharmacology Ion Kinases Kinases/*pharmacology Messenger/analysis Molecular Northern Phosphodiesterase Phosphorylation Protein Proteins/*genetics/isolation RNA, Receptor Regulation Sequence Transfection beta-Adrenergic beta/*drug effects/physiology purification/pharmacology Adrenergic
%N 4962
%P 1547-50
%T beta-Arrestin: a protein that regulates beta-adrenergic receptor
function
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2163110
%V 248
%X Homologous or agonist-specific desensitization of beta-adrenergic
receptors is thought to be mediated by a specific kinase, the beta-adrenergic
receptor kinase (beta ARK). However, recent data suggest that a cofactor
is required for this kinase to inhibit receptor function. The complementary
DNA for such a cofactor was cloned and found to encode a 418-amino
acid protein homologous to the retinal protein arrestin. The protein,
termed beta-arrestin, was expressed and partially purified. It inhibited
the signaling function of beta ARK-phosphorylated beta-adrenergic
receptors by more than 75 percent, but not that of rhodopsin. It
is proposed that beta-arrestin in concert with beta ARK effects homologous
desensitization of beta-adrenergic receptors.
@article{Lohse1990a,
abstract = {Homologous or agonist-specific desensitization of beta-adrenergic
receptors is thought to be mediated by a specific kinase, the beta-adrenergic
receptor kinase (beta ARK). However, recent data suggest that a cofactor
is required for this kinase to inhibit receptor function. The complementary
DNA for such a cofactor was cloned and found to encode a 418-amino
acid protein homologous to the retinal protein arrestin. The protein,
termed beta-arrestin, was expressed and partially purified. It inhibited
the signaling function of beta ARK-phosphorylated beta-adrenergic
receptors by more than 75 percent, but not that of rhodopsin. It
is proposed that beta-arrestin in concert with beta ARK effects homologous
desensitization of beta-adrenergic receptors.},
added-at = {2010-12-14T18:12:02.000+0100},
author = {Lohse, M. J. and Benovic, J. L. and Codina, J. and Caron, M. G. and Lefkowitz, R. J.},
biburl = {https://www.bibsonomy.org/bibtex/2ce53cf46fd7604e477c2d34e582945fc/pharmawuerz},
endnotereftype = {Journal Article},
interhash = {049947145666ea979957b7628ea0c31b},
intrahash = {ce53cf46fd7604e477c2d34e582945fc},
issn = {0036-8075 (Print) 0036-8075 (Linking)},
journal = {Science},
keywords = {& *Cyclic AMP-Dependent Acid Amino Animals Antigens/*genetics/isolation Arrestin Blotting, Chromatography, Cloning, DNA/genetics Data Exchange Expression Eye Gene Inhibitors/*pharmacology Ion Kinases Kinases/*pharmacology Messenger/analysis Molecular Northern Phosphodiesterase Phosphorylation Protein Proteins/*genetics/isolation RNA, Receptor Regulation Sequence Transfection beta-Adrenergic beta/*drug effects/physiology purification/pharmacology Adrenergic},
month = {Jun 22},
note = {Lohse, M J Benovic, J L Codina, J Caron, M G Lefkowitz, R J DK19318/DK/NIDDK
NIH HHS/United States HL16037/HL/NHLBI NIH HHS/United States Research
Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. United
states Science (New York, N.Y.) Science. 1990 Jun 22;248(4962):1547-50.},
number = 4962,
pages = {1547-50},
shorttitle = {beta-Arrestin: a protein that regulates beta-adrenergic receptor function},
timestamp = {2010-12-14T18:22:41.000+0100},
title = {beta-Arrestin: a protein that regulates beta-adrenergic receptor
function},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2163110},
volume = 248,
year = 1990
}