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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1994-6-2
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
343
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
120-4
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8168616-Amino Acid Sequence,
pubmed-meshheading:8168616-Animals,
pubmed-meshheading:8168616-Cell Line,
pubmed-meshheading:8168616-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:8168616-Eye Proteins,
pubmed-meshheading:8168616-GTP-Binding Protein Regulators,
pubmed-meshheading:8168616-GTP-Binding Proteins,
pubmed-meshheading:8168616-Humans,
pubmed-meshheading:8168616-Molecular Sequence Data,
pubmed-meshheading:8168616-Phosphoproteins,
pubmed-meshheading:8168616-Phosphorylation,
pubmed-meshheading:8168616-Signal Transduction,
pubmed-meshheading:8168616-beta-Adrenergic Receptor Kinases
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pubmed:year |
1994
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pubmed:articleTitle |
Phosducin inhibits receptor phosphorylation by the beta-adrenergic receptor kinase in a PKA-regulated manner.
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pubmed:affiliation |
Laboratory of Molecular Biology, University of Munich, Max-Planck-Institute of Biochemistry, Martinsried, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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