Regulators of G Protein Signaling Proteins as Determinants of the Rate of Desensitization of Presynaptic Calcium Channels

• Published in: The Journal of biological chemistry Vol. 274; no. 20; pp. 14490 - 14494
• Main Authors: Diversé-Pierluissi, Marı́a A., Fischer, Thierry, Jordan, J. Dedrick, Schiff, Max, Ortiz, Daniel F., Farquhar, Marilyn G., De Vries, Luc
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 14-05-1999; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Animals; binding; binding proteins; calcium; Calcium Channel Blockers - pharmacology; Calcium Channels - physiology; Cells, Cultured; Chick Embryo; chickens; dorsal root ganglia; electric current; Electrophysiology; ganglia; GTP Phosphohydrolases - physiology; GTP-Binding Proteins - physiology; GTPase-Activating Proteins; guanosine triphosphate; inorganic ions; interactions; ion transport; Molecular Sequence Data; Mollusk Venoms - pharmacology; neurons; Neurons - drug effects; Neurons - physiology; neurophysiology; norepinephrine; omega-Conotoxin GVIA; Peptides - pharmacology; Phosphoproteins - physiology; Presynaptic Terminals - drug effects; Presynaptic Terminals - physiology; Proteins - physiology; ras GTPase-Activating Proteins; ras Proteins - physiology; RGS Proteins; Signal Transduction
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.274.20.14490

Norepinephrine inhibits ω-conotoxin GVIA-sensitive presynaptic Ca2+ channels in chick dorsal root ganglion neurons through two pathways, one mediated by Go and the other by Gi. These pathways desensitize at different rates. We have found that recombinant Gα interacting protein (GAIP) and regulators of G protein signaling (RGS)4 selectively accelerate the rate of desensitization of Go- and Gi-mediated pathways, respectively. Blockade of endogenous RGS proteins using antibodies raised against Gα interacting protein and RGS4 slows the rate of desensitization of these pathways in a selective manner. These results demonstrate that different RGS proteins may interact with Gi and Go selectively, giving rise to distinct time courses of transmitter-mediated effects.