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Pureβ-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclase
Naturevolume 306, pages562–566 (1983)Cite this article
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Abstract
The β-adrenergic receptor binding subunits from frog erythrocytes, hamster lung and guinea pig lung have been purified to apparent homogeneity and in all cases reside on a single polypeptide. Insertion of the pure receptors into phospholipid vesicles and subsequent fusion of these vesicles with a receptor-deficient cell conveys β-adrenergic responsiveness to the adenylate cyclase system of the acceptor cell. Such responsiveness is linearly dependent on the amount of receptor used in the fusion experiments and is independent of the receptor source. Moreover, this responsiveness displays appropriate β-adrenergic specificity. These results indicate that the β-adrenergic receptor polypeptide contains both the ligand binding site and the site responsible for mediating stimulation of adenylate cyclase activity, presumably via interaction with the guanine nucleotide regulatory protein.
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Authors and Affiliations
Howard Hughes Medical Institute Research Laboratories, Departments of Medicine (Cardiology), Biochemistry and Physiology, Duke University Medical Center, Durham, North Carolina, 27710, USA
Richard A. Cerione, Berta Strulovici, Jeffrey L. Benovic, Robert J. Lefkowitz & Marc G. Caron
- Richard A. Cerione
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- Berta Strulovici
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- Jeffrey L. Benovic
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- Robert J. Lefkowitz
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- Marc G. Caron
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Cerione, R., Strulovici, B., Benovic, J.et al. Pureβ-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclase.Nature306, 562–566 (1983). https://doi.org/10.1038/306562a0
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