Evidence map›Paper›PMID 27247413›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Structural insight into photoactivation of an adenylate cyclase from a photosynthetic cyanobacterium.

Mio Ohki, Kanako Sugiyama, Fumihiro Kawai, Hitomi Tanaka, Yuuki Nihei, Satoru Unzai, Masumi Takebe, Shigeru Matsunaga, Shin-Ichi Adachi, Naoya Shibayama and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
16.4field-weighted citation impact, top 1% 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

43 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. An Integrated Optogenetic and Bioelectronic Platform for Regulating Cardiomyocyte Function.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Cardiac optogenetics: shining light on signaling pathways.Pflugers Archiv : European journal of physiology · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. The nature of proton-coupled electron transfer in a blue light using flavin domain.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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

17 authors at 7 institutions in 1 country.

Mio OhkiDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama, 230-0045, Japan;
Kanako SugiyamaDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama, 230-0045, Japan; Drug Design Group, Kanagawa Academy of Science and Technology, Takatsu, Kawasaki 213-0012, Japan;
Fumihiro KawaiDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama, 230-0045, Japan;
Hitomi TanakaFaculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, 274-8510, Japan;
Yuuki NiheiFaculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, 274-8510, Japan;
Satoru UnzaiDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama, 230-0045, Japan;
Masumi TakebeCentral Research Laboratory, Hamamatsu Photonics K.K., Hamamatsu, Shizuoka 434-8601, Japan;
Shigeru MatsunagaCentral Research Laboratory, Hamamatsu Photonics K.K., Hamamatsu, Shizuoka 434-8601, Japan;
Shin-Ichi AdachiInstitute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), 1-1 Oho, Tsukuba, Ibaraki 305-0801, Japan;
Naoya ShibayamaDivision of Biophysics, Department of Physiology, Jichi Medical University, Shimotsuke, Tochigi 329-0498, Japan;
Zhiwen ZhouLaboratory of Chemical Pharmacology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Ryuta KoyamaLaboratory of Chemical Pharmacology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.
Yuji IkegayaLaboratory of Chemical Pharmacology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan.ORCID 0000-0003-2260-8191
Tetsuo TakahashiFaculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, 274-8510, Japan;
Jeremy R H TameDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama, 230-0045, Japan;
Mineo IsekiFaculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, 274-8510, Japan; park@tsurumi.yokohama-cu.ac.jp mineo.iseki@phar.toho-u.ac.jp.
Sam-Yong ParkDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama, 230-0045, Japan; park@tsurumi.yokohama-cu.ac.jp mineo.iseki@phar.toho-u.ac.jp.
Yokohama City University · JPToho University · JPThe University of Tokyo · JPHamamatsu Photonics (Japan) · JPHigh Energy Accelerator Research Organization · JPJichi Medical University · JPKanagawa Academy of Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic-AMP is one of the most important second messengers, regulating many crucial cellular events in both prokaryotes and eukaryotes, and precise spatial and temporal control of cAMP levels by light shows great promise as a simple means of manipulating and studying numerous cell pathways and processes. The photoactivated adenylate cyclase (PAC) from the photosynthetic cyanobacterium Oscillatoria acuminata (OaPAC) is a small homodimer eminently suitable for this task, requiring only a simple flavin chromophore within a blue light using flavin (BLUF) domain. These domains, one of the most studied types of biological photoreceptor, respond to blue light and either regulate the activity of an attached enzyme domain or change its affinity for a repressor protein. BLUF domains were discovered through studies of photo-induced movements of Euglena gracilis, a unicellular flagellate, and gene expression in the purple bacterium Rhodobacter sphaeroides, but the precise details of light activation remain unknown. Here, we describe crystal structures and the light regulation mechanism of the previously undescribed OaPAC, showing a central coiled coil transmits changes from the light-sensing domains to the active sites with minimal structural rearrangement. Site-directed mutants show residues essential for signal transduction over 45 Å across the protein. The use of the protein in living human cells is demonstrated with cAMP-dependent luciferase, showing a rapid and stable response to light over many hours and activation cycles. The structures determined in this study will assist future efforts to create artificial light-regulated control modules as part of a general optogenetic toolkit.

Indexed as

Adenylyl CyclasesBacterial ProteinsCyclic AMPEnzyme ActivationHEK293 CellsHumansLightOscillatoriaProtein DomainsSecond Messenger SystemsStructure-Activity RelationshipAdenylyl CyclasesBacterial ProteinsCyclic AMPallosteryblue lightoptogeneticsX-ray crystallography

Identifiers

PMID27247413
PMCPMC4914150
OpenAlexW2415890418

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.