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
Language
- eng
Conference Location
- United States