Evidence map›Paper›PMID 10366613›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1999

Activity-dependent modulation of rod photoreceptor cyclic nucleotide-gated channels mediated by phosphorylation of a specific tyrosine residue.

E Molokanova, F Maddox, C W Luetje, R H Kramer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.1field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 57 citations in OpenAlex.

  1. Trial
  2. The solute carrier SLC9C1 is a NaNature communications · 2018
    Article
  3. Article
  4. Article
  5. Article
  6. Insulin receptor regulates photoreceptor CNG channel activity.American journal of physiology. Endocrinology and metabolism · 2012
    Article
  7. Article
  8. Review
  9. Regulation of ON bipolar cell activity.Progress in retinal and eye research · 2008
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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 · 2003
    Article
  15. Article
  16. Article
  17. Circadian phase-dependent modulation of cGMP-gated channels of cone photoreceptors by dopamine and D2 agonist.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
  18. Article
  19. Regulation of structural plasticity by different channel types in rod and cone photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

E MolokanovaDepartment of Molecular and Cellular Pharmacology, University of Miami School of Medicine, Miami, Florida 33101, USA.
F Maddox
C W Luetje
R H Kramer
University of Miami · US

Funding

BINDING SITE STRUCTURE OF NEURONAL NICOTINIC RECEPTORSR01DA008102 · NIDA · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LUETJE, CHARLES WARD · 1994 to 2002
$963k
SYNAPTIC FUNCTION OF CNG CHANNELS IN THE RETINAR01EY011877 · NEI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI KRAMER, RICHARD H · 1998 to 2001
$374k
NEI NIH HHS EY11877NIDA NIH HHS DA08102
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) channels are crucial for phototransduction in vertebrate rod photoreceptors. The cGMP sensitivity of these channels is modulated by diffusible intracellular messengers, including Ca2+/calmodulin, contributing to negative feedback during sensory adaptation. Membrane-associated protein tyrosine kinases and phosphatases also modulate rod CNG channels, but whether this results from direct changes in the phosphorylation state of the channel protein has been unclear. Here, we show that bovine rod CNG channel alpha-subunits (bRET) contain a tyrosine phosphorylation site crucial for modulation. bRET channels expressed in Xenopus oocytes exhibit modulation, whereas rat olfactory CNG channels (rOLF) do not. Chimeric channels reveal that differences in the C terminus, containing the cyclic nucleotide-binding domain, account for this difference. One specific tyrosine in bRET (Y498) appears to be crucial; replacement of this tyrosine in bRET curtails modulation, whereas installation into rOLF confers modulability. As the channel becomes dephosphorylated, there is an increase in the rate of spontaneous openings in the absence of ligand, indicating that changes in the phosphorylation state affect the allosteric gating equilibrium. Moreover, we find that dephosphorylation, which favors channel opening, requires open channels, whereas phosphorylation, which promotes channel closing, requires closed channels. Hence, modulation by changes in tyrosine phosphorylation is activity-dependent and may constitute a positive feedback mechanism, contrasting with negative feedback systems underlying adaptation.

Indexed as

Adenosine TriphosphateAllosteric RegulationAnimalsCattleCyclic AMPCyclic GMPCyclic Nucleotide-Gated Cation ChannelsIon Channel GatingIon ChannelsOocytesPatch-Clamp TechniquesPhosphorylationProtein-Tyrosine KinasesRetinal Rod Photoreceptor CellsTyrosineVision, OcularAdenosine TriphosphateCyclic AMPCyclic GMPCyclic Nucleotide-Gated Cation ChannelsIon ChannelsProtein-Tyrosine KinasesTyrosine

Identifiers

PMID10366613
PMCPMC6782659
OpenAlexW1496131947

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.