Evidence map›Paper›PMID 31501546›Full record

ArticleNature methods2019

FRET-assisted photoactivation of flavoproteins for in vivo two-photon optogenetics.

Tomoaki Kinjo, Kenta Terai, Shoichiro Horita, Norimichi Nomura, Kenta Sumiyama, Kaori Togashi, So Iwata, Michiyuki Matsuda

Abstract read
PubMed Publisher
In one paragraph

Article in Nature methods, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Design and engineering of light-sensitive protein switches.Current opinion in structural biology · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Multiphoton intravital microscopy of rodents.Nature reviews. Methods primers · 2022
    Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Visualization and Manipulation of Intracellular Signaling.Advances in experimental medicine and biology · 2021
    Review
  18. Article
  19. Article
  20. FRET-Based CaSensors (Basel, Switzerland) · 2020
    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

8 authors at 2 institutions in 2 countries.

Tomoaki KinjoDepartment of Pathology and Biology of Diseases, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Kenta TeraiResearch Center for Dynamic Living Systems, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0000-0001-7638-3720
Shoichiro HoritaDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
Norimichi NomuraDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0000-0002-6330-2239
Kenta SumiyamaLaboratory for Mouse Genetic Engineering, RIKEN Center for Biosystems Dynamics Research, Osaka, Japan.ORCID http://orcid.org/0000-0001-8785-5439
Kaori TogashiDepartment of Diagnostic Imaging and Nuclear Medicine, Graduate School of Medicine, Kyoto University, Kyoto, Japan.
So IwataDepartment of Cell Biology, Graduate School of Medicine, Kyoto University, Kyoto, Japan.ORCID http://orcid.org/0000-0003-1735-2937
Michiyuki MatsudaDepartment of Pathology and Biology of Diseases, Graduate School of Medicine, Kyoto University, Kyoto, Japan. matsuda.michiyuki.2c@kyoto-u.ac.jp.ORCID http://orcid.org/0000-0002-5876-9969
Kyoto University · JPRIKEN Center for Biosystems Dynamics Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Optical dimerizers have been developed to untangle signaling pathways, but they are of limited use in vivo, partly due to their inefficient activation under two-photon (2P) excitation. To overcome this problem, we developed Förster resonance energy transfer (FRET)-assisted photoactivation, or FRAPA. On 2P excitation, mTagBFP2 efficiently absorbs and transfers the energy to the chromophore of CRY2. Based on structure-guided engineering, a chimeric protein with 40% FRET efficiency was developed and named 2P-activatable CRY2, or 2paCRY2. 2paCRY2 was employed to develop a RAF1 activation system named 2paRAF. In three-dimensionally cultured cells expressing 2paRAF, extracellular signal-regulated kinase (ERK) was efficiently activated by 2P excitation at single-cell resolution. Photoactivation of ERK was also accomplished in the epidermal cells of 2paRAF-expressing mice. We further developed an mTFP1-fused LOV domain that exhibits efficient response to 2P excitation. Collectively, FRAPA will pave the way to single-cell optical control of signaling pathways in vivo.

Indexed as

OptogeneticsPhotonsAnimalsEnzyme ActivationExtracellular Signal-Regulated MAP KinasesFlavoproteinsFluorescence Resonance Energy TransferMiceExtracellular Signal-Regulated MAP KinasesFlavoproteins

Identifiers

PMID31501546
OpenAlexW2972914474

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.