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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lohse, M. J. Freund, S. Krasel, C. Winstel, R. Hoppe, E. |
| Description | Author Affiliation: Winstel R ( Laboratory of Molecular Biology, University of Munich, Germany.); |
| Abstract | The beta-adrenergic receptor kinase (betaARK) is the prototypical member of the family of cytosolic kinases that phosphorylate guanine nucleotide binding-protein-coupled receptors and thereby trigger uncoupling between receptors and guanine nucleotide binding proteins. Herein we show that this kinase is subject to phosphorylation and regulation by protein kinase C (PKC). In cell lines stably expressing alpha1B- adrenergic receptors, activation of these receptors by epinephrine resulted in an activation of cytosolic betaARK. Similar data were obtained in 293 cells transiently coexpressing alpha1B- adrenergic receptors and betaARK-1. Direct activation of PKC with phorbol esters in these cells caused not only an activation of cytosolic betaARK-1 but also a translocation of betaARK immunoreactivity from the cytosol to the membrane fraction. A PKC preparation purified from rat brain phospborylated purified recombinant betaARK-1 to a stoichiometry of 0.86 phosphate per betaARK-1. This phosphorylation resulted in an increased activity of betaARK-1 when membrane-bound rhodopsin served as its substrate but in no increase of its activity toward a soluble peptide substrate. The site of phosphorylation was mapped to the C terminus of betaARK-1. We conclude that PKC activates betaARK by enhancing its translocation to the plasma membrane. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 5 |
| Volume Number | 93 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1996-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cyclic AMP-Dependent Protein Kinases Metabolism Protein Kinase C Physiology Receptors, Adrenergic, Alpha-1 Amino Acid Sequence Animals CHO Cells Cell Compartmentation Cell Line Cell Membrane Enzymology Cricetinae Enzyme Activation Drug Effects Epinephrine Pharmacology Molecular Sequence Data Peptides Chemistry Phosphorylation Recombinant Proteins Signal Transduction Beta-Adrenergic Receptor Kinases Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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