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 Neuroscijournal_title
Nature neuroscienceauthors
Yevenes GE,Peoples RW,Tapia JC,Parodi J,Soto X,Olate J,Aguayo LGdoi
10.1038/nn1095subject
Has Abstractpub_date
2003-08-01 00:00:00pages
819-24issue
8eissn
1097-6256issn
1546-1726pii
nn1095journal_volume
6pub_type
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