Evidence map›Paper›PMID 31098413›Full record

ArticleCommunications biology2019

The counterion-retinylidene Schiff base interaction of an invertebrate rhodopsin rearranges upon light activation.

Takashi Nagata, Mitsumasa Koyanagi, Hisao Tsukamoto, Eshita Mutt, Gebhard F X Schertler, Xavier Deupi, Akihisa Terakita

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 72 citations in OpenAlex.

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  16. Dynamic Structural Biology Experiments at XFEL or Synchrotron Sources.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  17. Article
  18. Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. 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

7 authors at 2 institutions in 2 countries.

Takashi Nagata1Department of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka, 558-8585 Japan.ORCID 0000-0001-5379-2951
Mitsumasa Koyanagi1Department of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka, 558-8585 Japan.ORCID 0000-0002-7741-918X
Hisao Tsukamoto1Department of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka, 558-8585 Japan.
Eshita Mutt3Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.ORCID 0000-0003-3225-4761
Gebhard F X Schertler3Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.ORCID 0000-0002-5846-6810
Xavier Deupi3Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institute, CH-5232 Villigen PSI, Switzerland.ORCID 0000-0003-4572-9316
Akihisa Terakita1Department of Biology and Geosciences, Graduate School of Science, Osaka City University, Osaka, 558-8585 Japan.ORCID 0000-0002-8379-8913
Osaka City University · JPPaul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Animals sense light using photosensitive proteins-rhodopsins-containing a chromophore-retinal-that intrinsically absorbs in the ultraviolet. Visible light-sensitivity depends primarily on protonation of the retinylidene Schiff base (SB), which requires a negatively-charged amino acid residue-counterion-for stabilization. Little is known about how the most common counterion among varied rhodopsins, Glu181, functions. Here, we demonstrate that in a spider visual rhodopsin, orthologue of mammal melanopsins relevant to circadian rhythms, the Glu181 counterion functions likely by forming a hydrogen-bonding network, where Ser186 is a key mediator of the Glu181-SB interaction. We also suggest that upon light activation, the Glu181-SB interaction rearranges while Ser186 changes its contribution. This is in contrast to how the counterion of vertebrate visual rhodopsins, Glu113, functions, which forms a salt bridge with the SB. Our results shed light on the molecular mechanisms of visible light-sensitivity relevant to invertebrate vision and vertebrate non-visual photoreception.

Indexed as

Amino Acid SubstitutionAnimalsArthropod ProteinsHydrogen BondingLightModels, MolecularMutagenesis, Site-DirectedPhotochemical ProcessesProtein StabilityRhodopsinSchiff BasesSpidersArthropod ProteinsRhodopsinSchiff BasesG protein-coupled receptorsMolecular biophysics

Identifiers

PMID31098413
PMCPMC6513861
OpenAlexW2944529279

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.