%0 Journal Article %1 Hekman1994 %A Hekman, M. %A Bauer, P. H. %A Sohlemann, P. %A Lohse, M. J. %D 1994 %J FEBS Lett %K & AMP-Dependent Acid Amino Animals Cell Cyclic Data Eye GTP-Binding Humans Kinases Kinases/*antagonists Line Molecular Phosphoproteins/*pharmacology Phosphorylation Protein Proteins/*pharmacology Proteins/metabolism Receptor Regulators Sequence Signal Transduction beta-Adrenergic inhibitors/*metabolism %N 2 %P 120-4 %T Phosducin inhibits receptor phosphorylation by the beta-adrenergic receptor kinase in a PKA-regulated manner %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8168616 %V 343 %X Homologous or receptor-specific desensitization of beta-adrenergic receptors is thought to be triggered by receptor phosphorylation mediated by the beta-adrenergic receptor kinases (beta ARK). Upon receptor activation, cytosolic beta ARK translocates to the membrane, probably by binding to G-protein beta gamma-subunits. Using the purified proteins reconstituted into phospholipid vesicles we show here that this binding process can be inhibited by phosducin, a cytosolic protein that has recently been described as a regulator of G-protein-mediated signalling. Phosducin appears to complete very effectively with beta ARK for the G-protein beta gamma-subunits. These inhibitory effects of phosducin on receptor phosphorylation are antagonized following phosphorylation of phosducin by protein kinase A. It is proposed that phosducin may act as a regulator of homologous beta-adrenergic receptor desensitization.

@article{Hekman1994, abstract = {Homologous or receptor-specific desensitization of beta-adrenergic receptors is thought to be triggered by receptor phosphorylation mediated by the beta-adrenergic receptor kinases (beta ARK). Upon receptor activation, cytosolic beta ARK translocates to the membrane, probably by binding to G-protein beta gamma-subunits. Using the purified proteins reconstituted into phospholipid vesicles we show here that this binding process can be inhibited by phosducin, a cytosolic protein that has recently been described as a regulator of G-protein-mediated signalling. Phosducin appears to complete very effectively with beta ARK for the G-protein beta gamma-subunits. These inhibitory effects of phosducin on receptor phosphorylation are antagonized following phosphorylation of phosducin by protein kinase A. It is proposed that phosducin may act as a regulator of homologous beta-adrenergic receptor desensitization.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Hekman, M. and Bauer, P. H. and Sohlemann, P. and Lohse, M. J.}, biburl = {https://www.bibsonomy.org/bibtex/2044bd1f694ad1781379c1714fa39f5bf/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {fcc20fa28f27fedff5ed75af7598a049}, intrahash = {044bd1f694ad1781379c1714fa39f5bf}, issn = {0014-5793 (Print) 0014-5793 (Linking)}, journal = {FEBS Lett}, keywords = {& AMP-Dependent Acid Amino Animals Cell Cyclic Data Eye GTP-Binding Humans Kinases Kinases/*antagonists Line Molecular Phosphoproteins/*pharmacology Phosphorylation Protein Proteins/*pharmacology Proteins/metabolism Receptor Regulators Sequence Signal Transduction beta-Adrenergic inhibitors/*metabolism}, month = {Apr 25}, note = {Hekman, M Bauer, P H Sohlemann, P Lohse, M J Research Support, Non-U.S. Gov't Netherlands FEBS letters FEBS Lett. 1994 Apr 25;343(2):120-4.}, number = 2, pages = {120-4}, shorttitle = {Phosducin inhibits receptor phosphorylation by the beta-adrenergic receptor kinase in a PKA-regulated manner}, timestamp = {2010-12-14T18:18:55.000+0100}, title = {Phosducin inhibits receptor phosphorylation by the beta-adrenergic receptor kinase in a PKA-regulated manner}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8168616}, volume = 343, year = 1994 }