%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 }