ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2005
Selective modulation of neuronal nicotinic acetylcholine receptor channel subunits by Go-protein subunits.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- Article
- Article
- The α5 Nicotinic Acetylcholine Receptor Subunit Differentially Modulates α4β2Frontiers in synaptic neuroscience · 2020Review
- Feature Article: Selective modulation of tonically active GABAExperimental biology and medicine (Maywood, N.J.) · 2018Article
- Ethanol effects on glycinergic transmission: From molecular pharmacology to behavior responses.Pharmacological research · 2015Review
- Identification and Characterization of a G Protein-binding Cluster in α7 Nicotinic Acetylcholine Receptors.The Journal of biological chemistry · 2015Article
- Control of ethanol sensitivity of the glycine receptor α3 subunit by transmembrane 2, the intracellular splice cassette and C-terminal domains.The Journal of pharmacology and experimental therapeutics · 2015Article
- Microtubule dynamics at the growth cone are mediated by α7 nicotinic receptor activation of a Gαq and IP3 receptor pathway.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Connections of nicotine to cancer.Nature reviews. Cancer · 2014Review
- Axon targeting of the alpha 7 nicotinic receptor in developing hippocampal neurons by Gprin1 regulates growth.Journal of neurochemistry · 2014Article
- Electrophysiological and pharmacological evaluation of the nicotinic cholinergic system in chagasic rats.BMC pharmacology & toxicology · 2013Article
- Virtual screening against acetylcholine binding protein.Journal of biomolecular screening · 2012Article
- The basic property of Lys385 is important for potentiation of the human α1 glycine receptor by ethanol.The Journal of pharmacology and experimental therapeutics · 2012Article
- Activated G protein α s subunits increase the ethanol sensitivity of human glycine receptors.The Journal of pharmacology and experimental therapeutics · 2011Article
- Fast synaptic transmission in the goldfish CNS mediated by multiple nicotinic receptors.The Journal of physiology · 2011Article
- Molecular requirements for ethanol differential allosteric modulation of glycine receptors based on selective Gbetagamma modulation.The Journal of biological chemistry · 2010Article
- Homer1a-dependent crosstalk between NMDA and metabotropic glutamate receptors in mouse neurons.PloS one · 2010Article
- Blockade of ethanol-induced potentiation of glycine receptors by a peptide that interferes with Gbetagamma binding.The Journal of pharmacology and experimental therapeutics · 2009Article
- Coupling of ionic events to protein kinase signaling cascades upon activation of alpha7 nicotinic receptor: cooperative regulation of alpha2-integrin expression and Rho kinase activity.The Journal of biological chemistry · 2009Article
- Proteomic analysis of an alpha7 nicotinic acetylcholine receptor interactome.Journal of proteome research · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-protein modulation of neuronal nicotinic acetylcholine receptor (nAChR) channels in rat intrinsic cardiac ganglia was examined using dialyzed whole-cell and excised membrane patch-recording configurations. Cell dialysis with GTPgammaS increased the agonist affinity of nAChRs, resulting in a potentiation of nicotine-evoked whole-cell currents at low concentrations. ACh- and nicotine-evoked current amplitudes were increased approximately twofold in the presence of GTPgammaS. In inside-out membrane patches, the open probability (NP(o)) of nAChR-mediated unitary currents was reversibly increased fourfold after bath application of 0.2 mm GTPgammaS relative to control but was unchanged in the presence of GDPbetaS. The modulation of nAChR-mediated whole-cell currents was agonist specific; currents evoked by the cholinergic agonists ACh, nicotine, and 1,1-dimethyl-4-phenylpiperazinium iodide, but not cytisine or choline, were potentiated in the presence of GTPgammaS. The direct interaction between G-protein subunits and nAChRs was examined by bath application of either G(o)alpha or Gbetagamma subunits to inside-out membrane patches and in glutathione S-transferase pull-down and coimmunoprecipitation experiments. Bath application of 50 nm Gbetagamma increased the open probability of ACh-activated single-channel currents fivefold, whereas G(o)alpha (50 nm) produced no significant increase in NP(o). Neuronal nAChR subunits alpha3-alpha5 and beta2 exhibited a positive interaction with G(o)alpha and Gbetagamma, whereas beta4 and alpha7 failed to interact with either of the G-protein subunits. These results provide evidence for a direct interaction between nAChR and G-protein subunits, underlying the increased open probability of ACh-activated single-channel currents and potentiation of nAChR-mediated whole-cell currents in parasympathetic neurons of rat intrinsic cardiac ganglia.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.