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  • Title: A regulator of G protein signalling (RGS) protein confers agonist-dependent relaxation gating to a G protein-gated K+ channel.
    Author: Fujita S, Inanobe A, Chachin M, Aizawa Y, Kurachi Y.
    Journal: J Physiol; 2000 Jul 15; 526 Pt 2(Pt 2):341-7. PubMed ID: 10896722.
    Abstract:
    1. The effects of RGS4 on the voltage-dependent relaxation of G protein-gated K+ (KG) channels were examined by heterologous expression in Xenopus oocytes. 2. While the relaxation kinetics was unaffected by the acetylcholine concentration ([ACh]) in the absence of RGS4, it became dependent on [ACh] when RGS4 was co-expressed. 3. Kinetic analyses indicated that RGS4 confers to the KG channel a voltage-independent inhibitory gating mechanism, which was attenuated by ACh in a concentration-dependent fashion. 4. In vitro biochemical studies showed that RGS4 could bind to the protein complex containing KG channel subunits. 5. Since the native cardiac KG channel exhibited similar agonist-dependent relaxation kinetics to that mediated by RGS4, it is suggested that KG channel gating is a novel physiological target of RGS protein-mediated regulation.
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