Nature Neuroscience6, 819 - 824 (2003)
Published online: 13 July 2003; | doi:10.1038/nn1095
Modulation of glycine-activated ion channel function by G-protein subunits
Gonzalo E Yevenes1, Robert W Peoples2, Juan C Tapia1, Jorge Parodi1, Ximena Soto3, Juan Olate3
& Luis G Aguayo1
1
Laboratory of Neurophysiology, Department of Physiology, Box 160-C, University of Concepción, Chile.
2
Unit on Cellular Neuropharmacology, Laboratory of Molecular and Cellular Neurobiology, National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Park 5 Building., Room. 150, 12420 Parklawn Dr., Bethesda, Maryland 20892-8115, USA.
3
Laboratory of Molecular Genetics, Department of Molecular Biology, Box 160-C, University of Concepción, Chile.
Correspondence should be addressed to Luis G Aguayo laguayo@udec.cl
Glycine receptors (GlyRs), together with GABAA and nicotinic acetylcholine (ACh) receptors, form part of the ligand-activated ion channel superfamily and regulate the excitability of the mammalian brain stem and spinal cord. Here we report that the ability of the neurotransmitter glycine to gate recombinant and native ionotropic GlyRs is modulated by the G protein dimer (G). We found that the amplitude of the glycine-activated Cl- current was enhanced after application of purified G or after activation of a G protein−coupled receptor. Overexpression of three distinct G protein subunits (G), as well as the G scavenger peptide ct-GRK2, significantly blunted the effect of G protein activation. Single-channel recordings from isolated membrane patches showed that G increased the GlyR open probability (nPo). Our results indicate that this interaction of G with GlyRs regulates both motor and sensory functions in the central nervous system.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated
subunits
dimer (G
subunits (G
