Modulation of glycine-activated ion channel function by G-protein betagamma subunits.

Abstract:

:Glycine receptors (GlyRs), together with GABA(A) 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 betagamma dimer (Gbetagamma). We found that the amplitude of the glycine-activated Cl- current was enhanced after application of purified Gbetagamma or after activation of a G protein-coupled receptor. Overexpression of three distinct G protein alpha subunits (Galpha), as well as the Gbetagamma scavenger peptide ct-GRK2, significantly blunted the effect of G protein activation. Single-channel recordings from isolated membrane patches showed that Gbetagamma increased the GlyR open probability (nP(o)). Our results indicate that this interaction of Gbetagamma with GlyRs regulates both motor and sensory functions in the central nervous system.

journal_name

Nat Neurosci

journal_title

Nature neuroscience

authors

Yevenes GE,Peoples RW,Tapia JC,Parodi J,Soto X,Olate J,Aguayo LG

doi

10.1038/nn1095

subject

Has Abstract

pub_date

2003-08-01 00:00:00

pages

819-24

issue

8

eissn

1097-6256

issn

1546-1726

pii

nn1095

journal_volume

6

pub_type

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