Evidence map›Paper›PMID 35710843›Full record

ArticleNature structural & molecular biology2022

Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels.

Andrey Rozenberg, Igor Kaczmarczyk, Donna Matzov, Johannes Vierock, Takashi Nagata, Masahiro Sugiura, Kota Katayama, Yuma Kawasaki, Masae Konno, Yujiro Nagasaka and 22 more

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In one paragraph

Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Apusomonad rhodopsins: A new family of ultraviolet to blue light-absorbing rhodopsin channels.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Harnessing light the retinal way.Nature chemistry · 2025
    Article
  5. Multistep 11-Journal of the American Chemical Society · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Photoisomerization pathway of the microbial rhodopsin chromophore in solution.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024
    Article
  14. Article
  15. Multiple retinal isomerizations during the early phase of the bestrhodopsin photoreaction.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Optogenetics meets physiology.Pflugers Archiv : European journal of physiology · 2023
    Article
  19. Diversity of rhodopsin cyclases in zoospore-forming fungi.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

32 authors at 8 institutions in 3 countries.

Andrey Rozenberg *Faculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel.ORCID 0000-0001-9534-2297
Igor Kaczmarczyk *Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Donna Matzov *Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Johannes Vierock *Institute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID 0000-0001-7368-5539
Takashi NagataThe Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan.
Masahiro SugiuraDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0002-4490-6336
Kota KatayamaPRESTO, Japan Science and Technology Agency, Kawaguchi, Japan.ORCID 0000-0001-8498-4374
Yuma KawasakiThe Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan.
Masae KonnoThe Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan.ORCID 0000-0002-0605-1816
Yujiro NagasakaThe Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan.
Mako AoyamaDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.
Ishita DasDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, Israel.
Efrat PahimaFritz Haber Center for Molecular Dynamics Research Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.
Jonathan ChurchFritz Haber Center for Molecular Dynamics Research Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.ORCID 0000-0001-5986-1305
Suliman AdamFritz Haber Center for Molecular Dynamics Research Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.ORCID 0000-0002-0891-5008
Veniamin A BorinFritz Haber Center for Molecular Dynamics Research Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.
Ariel ChazanFaculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel.
Sandra AugustinInstitute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.
Jonas WietekDepartment of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0002-8079-7042
Julien DineDepartment of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0001-6381-8916
Yoav PelegStructural Proteomics Unit (SPU), Life Sciences Core Facilities (LSCF), Weizmann Institute of Science, Rehovot, Israel.
Akira KawanabeLaboratory of Molecular Physiology & Biophysics, Faculty of Medicine, Kagawa University, Miki-cho, Japan.ORCID 0000-0002-1094-6209
Yuichiro FujiwaraLaboratory of Molecular Physiology & Biophysics, Faculty of Medicine, Kagawa University, Miki-cho, Japan.
Ofer YizharDepartment of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.ORCID 0000-0003-4228-1448
Mordechai ShevesDepartment of Molecular Chemistry and Materials Science, Weizmann Institute of Science, Rehovot, Israel.
Igor SchapiroFritz Haber Center for Molecular Dynamics Research Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.ORCID 0000-0001-8536-6869
Yuji FurutaniDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0001-5284-8773
Hideki KandoriDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Showa-ku, Japan.ORCID 0000-0002-4922-1344
Keiichi InoueThe Institute for Solid State Physics, The University of Tokyo, Kashiwa, Japan.ORCID 0000-0002-6898-4347
Peter HegemannInstitute for Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.ORCID 0000-0003-3589-6452
Oded BéjàFaculty of Biology, Technion - Israel Institute of Technology, Haifa, Israel. beja@technion.ac.il.ORCID 0000-0001-6629-0192
Moran Shalev-BenamiDepartment of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel. moransb@weizmann.ac.il.ORCID 0000-0001-6902-1924
Weizmann Institute of Science · ILHebrew University of Jerusalem · ILNagoya Institute of Technology · JPHumboldt-Universität zu Berlin · DETechnion – Israel Institute of Technology · ILThe University of Tokyo · JPJapan Science and Technology Agency · JPKagawa University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many organisms sense light using rhodopsins, photoreceptive proteins containing a retinal chromophore. Here we report the discovery, structure and biophysical characterization of bestrhodopsins, a microbial rhodopsin subfamily from marine unicellular algae, in which one rhodopsin domain of eight transmembrane helices or, more often, two such domains in tandem, are C-terminally fused to a bestrophin channel. Cryo-EM analysis of a rhodopsin-rhodopsin-bestrophin fusion revealed that it forms a pentameric megacomplex (~700 kDa) with five rhodopsin pseudodimers surrounding the channel in the center. Bestrhodopsins are metastable and undergo photoconversion between red- and green-absorbing or green- and UVA-absorbing forms in the different variants. The retinal chromophore, in a unique binding pocket, photoisomerizes from all-trans to 11-cis form. Heterologously expressed bestrhodopsin behaves as a light-modulated anion channel.

Indexed as

Ion ChannelsRhodopsinBestrophinsBestrophinsIon ChannelsRhodopsin

Identifiers

PMID35710843
OpenAlexW4282964081

What OpenQuestion holds

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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.