ArticleThe Journal of physiology1996
The action of cytoplasmic calcium on the cGMP-activated channel in salamander rod photoreceptors.
Article in The Journal of physiology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mathematical analysis of phototransduction reaction parameters in rods and cones.Scientific reports · 2022Article
- The structure of the native CNGA1/CNGB1 CNG channel from bovine retinal rods.Nature structural & molecular biology · 2022Article
- Functional modulation of phosphodiesterase-6 by calcium in mouse rod photoreceptors.Scientific reports · 2021Article
- Two structural components in CNGA3 support regulation of cone CNG channels by phosphoinositides.The Journal of general physiology · 2013Article
- Speed, sensitivity, and stability of the light response in rod and cone photoreceptors: facts and models.Progress in retinal and eye research · 2012Review
- CNG-modulin: a novel Ca-dependent modulator of ligand sensitivity in cone photoreceptor cGMP-gated ion channels.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Speed, adaptation, and stability of the response to light in cone photoreceptors: the functional role of Ca-dependent modulation of ligand sensitivity in cGMP-gated ion channels.The Journal of general physiology · 2012Article
- High cGMP synthetic activity in carp cones.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Dynamics of Ca2+-calmodulin-dependent inhibition of rod cyclic nucleotide-gated channels measured by patch-clamp fluorometry.The Journal of general physiology · 2004Article
- In intact mammalian photoreceptors, Ca2+-dependent modulation of cGMP-gated ion channels is detectable in cones but not in rods.The Journal of general physiology · 2004Article
- Tyrosine phosphorylation of rod cyclic nucleotide-gated channels switches off Ca2+/calmodulin inhibition.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- Multiple steps of phosphorylation of activated rhodopsin can account for the reproducibility of vertebrate rod single-photon responses.The Journal of general physiology · 2003Article
- Two temporal phases of light adaptation in retinal rods.The Journal of general physiology · 2002Article
- Fraction of the dark current carried by Ca(2+) through cGMP-gated ion channels of intact rod and cone photoreceptors.The Journal of general physiology · 2000Article
- Time course and Ca(2+) dependence of sensitivity modulation in cyclic GMP-gated currents of intact cone photoreceptors.The Journal of general physiology · 2000Article
- Molecular determinants of the modulation of cyclic nucleotide-activated channels by calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- In intact cone photoreceptors, a Ca2+-dependent, diffusible factor modulates the cGMP-gated ion channels differently than in rods.The Journal of general physiology · 1998Article
- Calmodulin controls the rod photoreceptor CNG channel through an unconventional binding site in the N-terminus of the beta-subunit.The EMBO journal · 1998Article
- Calcium modulation of ligand affinity in the cyclic GMP-gated ion channels of cone photoreceptors.The Journal of general physiology · 1997Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. Truncated salamander rod photoreceptors were internally perfused to investigate the action of cytoplasmic Ca2+ on cGMP-activated channels in the outer segment. 2. Switching from 1 microM Ca2+ to 0 Ca2+ increased the cGMP-activated current by a factor of 7.1 +/- 0.5 when measured in the first 60 s after the outer segment was opened to the bath, but only 2-fold after 5 min or more. This was attributed to the loss from the outer segment of a soluble factor required for Ca2+ to inhibit the cGMP-activated channel. 3. Short exposures to 0 Ca2+ caused an irreversible increase in the cGMP-activated current measured in 1 microM Ca2+, indicating that lowering [Ca2+] accelerated the loss of the channel inhibitor from the outer segment. 4. Channel activation occurred with a half-time of 6.7 s on switching to 0 Ca2+. Replacing 1 microM Ca2+ inhibited the current again with a half-time of 11.0 s. 5. The inhibition of the cGMP-activated current by Ca2+ could be described by a Hill curve with half-maximal suppression at 55 +/- 13 nM Ca2+ and a Hill coefficient of 1.4 +/- 0.4. 6. Addition of calmodulin (1 microM), or the calmodulin inhibitors mastoparan and calmidazolium (5 microM), did not alter the action of Ca2+ on the cGMP-activated current. 7. The increased affinity of the cGMP-activated channels in response to a fall in [Ca2+] has the magnitude, speed and Ca2+ dependence to suggest that it will promote recovery of the cGMP-activated current in response to the light-induced fall in [Ca2+] that normally occurs inside the outer segment.
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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.