Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptors.

Journal Article (Journal Article)

The actions of many hormones and neurotransmitters are mediated by the members of a superfamily of receptors coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins). These receptors are characterized by a highly conserved topographical arrangement in which seven transmembrane domains are connected by intracellular and extracellular loops. The interaction between these receptors and G proteins is mediated in large part by the third intracellular loop of the receptor. Coexpression of the third intracellular loop of the alpha 1B-adrenergic receptor with its parent receptor inhibited receptor-mediated activation of phospholipase C. The inhibition extended to the closely related alpha 1C-adrenergic receptor subtype, but not the phospholipase C-coupled M1 muscarinic acetylcholine receptor nor the adenylate cyclase-coupled D1A dopamine receptor. These results suggest that the receptor-G protein interface may represent a target for receptor antagonist drugs.

Full Text

Duke Authors

Cited Authors

  • Luttrell, LM; Ostrowski, J; Cotecchia, S; Kendall, H; Lefkowitz, RJ

Published Date

  • March 5, 1993

Published In

Volume / Issue

  • 259 / 5100

Start / End Page

  • 1453 - 1457

PubMed ID

  • 8383880

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.8383880


  • eng

Conference Location

  • United States