Evidence map›Paper›PMID 23479626›Full record

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

Homologs of vertebrate Opn3 potentially serve as a light sensor in nonphotoreceptive tissue.

Mitsumasa Koyanagi, Eiichiro Takada, Takashi Nagata, Hisao Tsukamoto, Akihisa Terakita

Open access · bronzeAbstract 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 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
6.0field-weighted citation impact, top 2% 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

86 citing papers in PubMed, 195 citations in OpenAlex.

  1. Review
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  5. Article
  6. The physiological functions of OPN5m.Eye and vision (London, England) · 2025
    Review
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  12. Hypothalamic opsin 3 suppresses MC4R signaling and potentiates Kir7.1 to promote food consumption.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
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  19. Review
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26 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Mitsumasa KoyanagiDepartment of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan.
Eiichiro Takada
Takashi Nagata
Hisao Tsukamoto
Akihisa Terakita
Osaka City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most opsins selectively bind 11-cis retinal as a chromophore to form a photosensitive pigment, which underlies various physiological functions, such as vision and circadian photoentrainment. Recently, opsin 3 (Opn3), originally called encephalopsin or panopsin, and its homologs were identified in various tissues including brain, eye, and liver in both vertebrates and invertebrates, including human. Because Opn3s are mainly expressed in tissues that are not considered to contain sufficient amounts of 11-cis retinal to form pigments, the photopigment formation ability of Opn3 has been of interest. Here, we report the successful expression of Opn3 homologs, pufferfish teleost multiple tissue opsin (PufTMT) and mosquito Opn3 (MosOpn3) and show that these proteins formed functional photopigments with 11-cis and 9-cis retinals. The PufTMT- and MosOpn3-based pigments have absorption maxima in the blue-to-green region and exhibit a bistable nature. These Opn3 homolog-based pigments activate Gi-type and Go-type G proteins light dependently, indicating that they potentially serve as light-sensitive Gi/Go-coupled receptors. We also demonstrated that mammalian cultured cells transfected with the MosOpn3 or PufTMT became light sensitive without the addition of 11-cis retinal and the photosensitivity retained after the continuous light exposure, showing a reusable pigment formation with retinal endogenously contained in culture medium. Interestingly, we found that the MosOpn3 also acts as a light sensor when constituted with 13-cis retinal, a ubiquitously present retinal isomer. Our findings suggest that homologs of vertebrate Opn3 might function as photoreceptors in various tissues; furthermore, these Opn3s, particularly the mosquito homolog, could provide a promising optogenetic tool for regulating cAMP-related G protein-coupled receptor signalings.

Indexed as

AnophelesTetraodontiformesAnimalsBase SequenceFish ProteinsGTP-Binding Protein alpha Subunits, Gi-GoHEK293 CellsHumansInsect ProteinsLightMolecular Sequence DataOpsinsReceptors, G-Protein-CoupledRetinaldehydeSequence Homology, Amino AcidSignal TransductionFish ProteinsGTP-Binding Protein alpha Subunits, Gi-GoInsect ProteinsOpsinsReceptors, G-Protein-CoupledRetinaldehyde

Identifiers

PMID23479626
PMCPMC3612648
OpenAlexW2025138486

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.