Pure beta-adrenergic receptor: the single polypeptide confers catecholamine responsiveness to adenylate cyclase.

Published

Journal Article

The beta-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 beta-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 beta-adrenergic specificity. These results indicate that the beta-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.

Full Text

Duke Authors

Cited Authors

  • Cerione, RA; Strulovici, B; Benovic, JL; Lefkowitz, RJ; Caron, MG

Published Date

  • December 8, 1983

Published In

Volume / Issue

  • 306 / 5943

Start / End Page

  • 562 - 566

PubMed ID

  • 6316161

Pubmed Central ID

  • 6316161

International Standard Serial Number (ISSN)

  • 0028-0836

Language

  • eng

Conference Location

  • England