ArticleBiophysical journal2000
Coexpression of alpha and beta subunits of the rod cyclic GMP-gated channel restores native sensitivity to cyclic AMP: role of D604/N1201.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- A case of retinitis pigmentosa homozygous for a rare CNGA1 causal variant.Scientific reports · 2021Article
- Disease-associated mutations in CNGB3 promote cytotoxicity in photoreceptor-derived cells.Molecular vision · 2013Article
- Restoration of proper trafficking to the cell surface for membrane proteins harboring cysteine mutations.PloS one · 2012Article
- The glutamic acid-rich protein is a gating inhibitor of cyclic nucleotide-gated channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- The retinitis pigmentosa mutation c.3444+1G>A in CNGB1 results in skipping of exon 32.PloS one · 2010Article
- Access of quaternary ammonium blockers to the internal pore of cyclic nucleotide-gated channels: implications for the location of the gate.The Journal of general physiology · 2006Article
- Subunit contributions to phosphorylation-dependent modulation of bovine rod cyclic nucleotide-gated channels.The Journal of physiology · 2003Article
- Influence of permeant ions on gating in cyclic nucleotide-gated channels.The Journal of general physiology · 2003Article
- Gating of heteromeric retinal rod channels by cyclic AMP: role of the C-terminal and pore domains.Biophysical journal · 2002Article
- Efficient coupling of ligand binding to channel opening by the binding domain of a modulatory (beta) subunit of the olfactory cyclic nucleotide-gated channel.The Journal of general physiology · 2001Article
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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
Coexpression of the betawt and alphawt subunits of the bovine rod channel restores two characteristics of the native channels: higher sensitivity to cAMP and potentiation of cGMP-induced currents by low cAMP concentrations. To test whether the increased sensitivity to cAMP is due to the uncharged nature of the asparagine residue (N1201) situated in place of aspartate D604 in the beta subunit as previously suggested (, Neuron. 15:619-625), we compared currents from wild-type (alphawt and alphawt/betawt) and from mutated channels (alphaD604N, alphaD604N/betawt, and alphawt/betaN1201D). The results show that the sensitivity to cAMP and cAMP potentiation is partly but not entirely determined by the charge of residue 1201 in the beta subunit. The D604N mutation in the alpha subunit and, to a lesser extent, coexpression of the betawt subunit with the alphawt subunit reduce the open probability for cGMP compared to that of the alphawt channel. Interpretation of the data with the MWC allosteric model (model of Monod, Wyman, Changeux;, J. Mol. Biol. 12:88-118) suggests that the D604N mutation in the alpha subunits and coassembly of alpha and beta subunits alter the free energy of gating by cAMP more than that of cAMP binding.
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