%0 Journal Article %1 Bauer1992 %A Bauer, P. H. %A Muller, S. %A Puzicha, M. %A Pippig, S. %A Obermaier, B. %A Helmreich, E. J. %A Lohse, M. J. %D 1992 %J Nature %K Acid Adenylate Amino Animals Brain/physiology Cyclase/metabolism Data Expression Eye GTP GTP-Binding Gene Kinases/*metabolism Messenger/genetics Molecular Phosphohydrolases/metabolism Phosphoproteins/*physiology Protein Proteins/*physiology RNA, Regulators Sequence Signal Transduction beta/physiology Receptor Proteins/metabolism Adrenergic %N 6381 %P 73-6 %T Phosducin is a protein kinase A-regulated G-protein regulator %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1319556 %V 358 %X Signal transduction by G-protein-coupled receptors is regulated by various mechanisms acting at the receptor level; those studied most thoroughly are from the beta-adrenergic receptor/Gs/adenylyl cyclase system. We report here a regulatory mechanism occurring at the level of the G proteins themselves. A protein with M(r) 33,000 that inhibits Gs-GTPase activity was purified from bovine brain. This protein is very similar or identical to phosducin, a protein previously thought to be specific for retina and pineal gland. Recombinant phosducin inhibited the GTPase activity of several G proteins, and also inhibited Gs-mediated adenylyl cyclase activation. Blockade of its inhibitory effects by protein kinase A suggests that phosducin may be part of a complex regulatory network controlling G-protein-mediated signalling.

@article{Bauer1992, abstract = {Signal transduction by G-protein-coupled receptors is regulated by various mechanisms acting at the receptor level; those studied most thoroughly are from the beta-adrenergic receptor/Gs/adenylyl cyclase system. We report here a regulatory mechanism occurring at the level of the G proteins themselves. A protein with M(r) 33,000 that inhibits Gs-GTPase activity was purified from bovine brain. This protein is very similar or identical to phosducin, a protein previously thought to be specific for retina and pineal gland. Recombinant phosducin inhibited the GTPase activity of several G proteins, and also inhibited Gs-mediated adenylyl cyclase activation. Blockade of its inhibitory effects by protein kinase A suggests that phosducin may be part of a complex regulatory network controlling G-protein-mediated signalling.}, added-at = {2010-12-14T18:12:02.000+0100}, author = {Bauer, P. H. and Muller, S. and Puzicha, M. and Pippig, S. and Obermaier, B. and Helmreich, E. J. and Lohse, M. J.}, biburl = {https://www.bibsonomy.org/bibtex/2653362e267f9ce2a5b7247c26d2f7256/pharmawuerz}, endnotereftype = {Journal Article}, interhash = {77ea3dfbee1640c0538f735a17983df7}, intrahash = {653362e267f9ce2a5b7247c26d2f7256}, issn = {0028-0836 (Print) 0028-0836 (Linking)}, journal = {Nature}, keywords = {Acid Adenylate Amino Animals Brain/physiology Cyclase/metabolism Data Expression Eye GTP GTP-Binding Gene Kinases/*metabolism Messenger/genetics Molecular Phosphohydrolases/metabolism Phosphoproteins/*physiology Protein Proteins/*physiology RNA, Regulators Sequence Signal Transduction beta/physiology Receptor Proteins/metabolism Adrenergic}, month = {Jul 2}, note = {Bauer, P H Muller, S Puzicha, M Pippig, S Obermaier, B Helmreich, E J Lohse, M J Research Support, Non-U.S. Gov't England Nature Nature. 1992 Jul 2;358(6381):73-6.}, number = 6381, pages = {73-6}, shorttitle = {Phosducin is a protein kinase A-regulated G-protein regulator}, timestamp = {2010-12-14T18:22:38.000+0100}, title = {Phosducin is a protein kinase A-regulated G-protein regulator}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1319556}, volume = 358, year = 1992 }