Evidence map›Paper›PMID 7556088›Full record

ArticleThe EMBO journal1995

Calmodulin binding to Drosophila NinaC required for termination of phototransduction.

J A Porter, B Minke, C Montell

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Regulation of arrestin translocation by Ca2+ and myosin III in Drosophila photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  5. Review
  6. Article
  7. Dopaminergic modulation of ganglion-cell photoreceptors in rat.The European journal of neuroscience · 2012
    Article
  8. Characteristics of light chains of Chara myosin revealed by immunological investigation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012
    Article
  9. Article
  10. Dependence on a retinophilin/myosin complex for stability of PKC and INAD and termination of phototransduction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    Article
  11. Why Drosophila to study phototransduction?Journal of neurogenetics · 2010
    Article
  12. Article
  13. Article
  14. Article
  15. Phototransduction and retinal degeneration in Drosophila.Pflugers Archiv : European journal of physiology · 2007
    Review
  16. Article
  17. Article
  18. Modulation of the light response by cAMP in Drosophila photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    Article
  19. Article
  20. Review
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

3 authors at 2 institutions in 1 country.

J A PorterDepartment of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA.
B Minke
C Montell
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

Unconventional roles for opsinsR01EY008117 · NEI · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI MONTELL, CRAIG · 1989 to 2022
$8.2M
NEI NIH HHS EY08117
6 · The paper itself

Abstract

The ninaC locus encodes two unconventional myosins, p132 and p174, consisting of fused protein kinase and myosin head domains expressed in Drosophila photoreceptor cells. NinaC are the major calmodulin-binding proteins in the retina and the NinaC-calmodulin interaction is required for the normal subcellular localization of calmodulin as well as for normal photo-transduction. In the current report, we present evidence for two calmodulin-binding sites in NinaC, C1 and C2, which have different in vitro binding properties. C1 was found to be common to both p132 and p174 while C2 was unique to p174. To address the requirements for calmodulin binding at each site in vivo, we generated transgenic flies expressing ninaC genes deleted for either C1 or C2. We found that the spatial localization of calmodulin depended on binding to both C1 and C2. Furthermore, mutation of either site resulted in a defective photoresponse. A prolonged depolarization afterpotential (PDA) was elicited at lower light intensities than necessary to produce a PDA in wild-type flies. These results suggest that calmodulin binding to both C1 and C2 is required in vivo for termination of phototransduction.

Indexed as

Drosophila ProteinsOcular Physiological PhenomenaAmino Acid SequenceAnimalsAnimals, Genetically ModifiedBase SequenceBinding SitesCalciumCalmodulinDrosophilaElectroretinographyEyeEye ProteinsFluorescent Antibody Technique, IndirectLightMembrane PotentialsCalciumCalmodulinDrosophila ProteinsEye ProteinsMyosin Heavy ChainsninaC protein, Drosophila

Identifiers

PMID7556088
PMCPMC394537
OpenAlexW121680641

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.