Evidence map›Paper›PMID 23536301›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Fly cryptochrome and the visual system.

Gabriella Mazzotta, Alessandro Rossi, Emanuela Leonardi, Moyra Mason, Cristiano Bertolucci, Laura Caccin, Barbara Spolaore, Alberto J M Martin, Matthias Schlichting, Rudi Grebler and 4 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed, 2 pooled it
2.2field-weighted citation impact, top 13% 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

49 citing papers in PubMed, 2 syntheses or guidelines pooled it, 80 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. A PDZ scaffolding/CaM-mediated pathway in Cryptochrome signaling.Protein science : a publication of the Protein Society · 2024
    Article
  11. Article
  12. Article
  13. AnInsects · 2023
    Article
  14. Article
  15. Review
  16. Why is it so difficult to study magnetic compass orientation in murine rodents?Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2022
    Review
  17. Human circadian variations.The Journal of clinical investigation · 2021
    Review
  18. Cryptochromes: Photochemical and structural insight into magnetoreception.Protein science : a publication of the Protein Society · 2021
    Review
  19. Review
  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

14 authors at 3 institutions in 2 countries.

Gabriella MazzottaDepartment of Biology, University of Padova, 35131 Padova, Italy.
Alessandro Rossi
Emanuela Leonardi
Moyra Mason
Cristiano Bertolucci
Laura Caccin
Barbara Spolaore
Alberto J M Martin
Matthias Schlichting
Rudi Grebler
Charlotte Helfrich-Förster
Stefano Mammi
Rodolfo Costa
Silvio C E Tosatto
University of Padua · ITUniversity of Würzburg · DEUniversity of Ferrara · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cryptochromes are flavoproteins, structurally and evolutionarily related to photolyases, that are involved in the development, magnetoreception, and temporal organization of a variety of organisms. Drosophila CRYPTOCHROME (dCRY) is involved in light synchronization of the master circadian clock, and its C terminus plays an important role in modulating light sensitivity and activity of the protein. The activation of dCRY by light requires a conformational change, but it has been suggested that activation could be mediated also by specific "regulators" that bind the C terminus of the protein. This C-terminal region harbors several protein-protein interaction motifs, likely relevant for signal transduction regulation. Here, we show that some functional linear motifs are evolutionarily conserved in the C terminus of cryptochromes and that class III PDZ-binding sites are selectively maintained in animals. A coimmunoprecipitation assay followed by mass spectrometry analysis revealed that dCRY interacts with Retinal Degeneration A (RDGA) and with Neither Inactivation Nor Afterpotential C (NINAC) proteins. Both proteins belong to a multiprotein complex (the Signalplex) that includes visual-signaling molecules. Using bioinformatic and molecular approaches, dCRY was found to interact with Neither Inactivation Nor Afterpotential C through Inactivation No Afterpotential D (INAD) in a light-dependent manner and that the CRY-Inactivation No Afterpotential D interaction is mediated by specific domains of the two proteins and involves the CRY C terminus. Moreover, an impairment of the visual behavior was observed in fly mutants for dCRY, indicative of a role, direct or indirect, for this photoreceptor in fly vision.

Indexed as

Amino Acid MotifsAnimalsBinding SitesComputational BiologyCryptochromesDrosophila melanogasterDrosophila ProteinsElectroretinographyEye ProteinsFlavoproteinsLightMass SpectrometryProtein Interaction MappingSignal TransductionTwo-Hybrid System TechniquesVision, Ocularcry protein, DrosophilaCryptochromesDrosophila ProteinsEye ProteinsFlavoproteins

Identifiers

PMID23536301
PMCPMC3625353
OpenAlexW2144507621

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.