Evidence map›Paper›PMID 31953223›Full record

ArticleMolecular plant2020

Photooligomerization Determines Photosensitivity and Photoreactivity of Plant Cryptochromes.

Qing Liu, Tiantian Su, Wenjin He, Huibo Ren, Siyuan Liu, Yadi Chen, Lin Gao, Xiaohua Hu, Haoyue Lu, Shijiang Cao and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
13.9field-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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Pooled it
  2. Key residues Tyr293, Val360, and Tyr399 regulate flavin stability in the plant cryptochrome from Chlamydomonas reinhardtii.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
    Article
  3. Review
  4. Article
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  7. Article
  8. Article
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  11. Review
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  14. SpSIZ1 from hyperaccumulatorFrontiers in plant science · 2024
    Article
  15. Review
  16. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Review
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

14 authors at 3 institutions in 2 countries.

Qing LiuBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Tiantian SuDepartment of Molecular, Cell & Developmental Biology, University of California, Los Angeles, CA 90095, USA.
Wenjin HeCollege of Life Sciences, Fujian Normal University, Fuzhou 350108, China.
Huibo RenBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Siyuan LiuBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Yadi ChenBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Lin GaoBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Xiaohua HuBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Haoyue LuBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Shijiang CaoCollege of Forestry, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Ying HuangBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Xu WangDepartment of Molecular, Cell & Developmental Biology, University of California, Los Angeles, CA 90095, USA.
Qin WangBasic Forestry and Proteomics Research Center, UCLA-FAFU Joint Research Center on Plant Proteomics, College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China. Electronic address: eva.wangqin@gmail.com.
Chentao LinDepartment of Molecular, Cell & Developmental Biology, University of California, Los Angeles, CA 90095, USA.
Fujian Agriculture and Forestry University · CNUniversity of California, Los Angeles · USFujian Normal University · CN

Funding

The signaling mechanisms of Arabidopsis CRY2R01GM056265 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LIN, CHENTAO · 2001 to 2021
$9.5M
PLANT PHOTOSENSORY RECEPTOR CRY2--SIGNALING MECHANISMR29GM056265 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LIN, CHENTAO · 1997 to 2001
$204k
NIGMS NIH HHS R01 GM056265NIGMS NIH HHS R29 GM056265
6 · The paper itself

Abstract

Plant and non-plant species possess cryptochrome (CRY) photoreceptors to mediate blue light regulation of development or the circadian clock. The blue light-dependent homooligomerization of Arabidopsis CRY2 is a known early photoreaction necessary for its functions, but the photobiochemistry and function of light-dependent homooligomerization and heterooligomerization of cryptochromes, collectively referred to as CRY photooligomerization, have not been well established. Here, we show that photooligomerization is an evolutionarily conserved photoreaction characteristic of CRY photoreceptors in plants and some non-plant species. Our analyses of the kinetics of the forward and reverse reactions of photooligomerization of Arabidopsis CRY1 and CRY2 provide a previously unrecognized mechanism underlying the different photosensitivity and photoreactivity of these two closely related photoreceptors. We found that photooligomerization is necessary but not sufficient for the functions of CRY2, implying that CRY photooligomerization is presumably accompanied by additional function-empowering conformational changes. We further demonstrated that the CRY2-CRY1 heterooligomerization plays roles in regulating functions of Arabidopsis CRYs in vivo. Taken together, these results suggest that photooligomerization is an evolutionarily conserved mechanism determining the photosensitivity and photoreactivity of plant CRYs.

Indexed as

LightArabidopsisCryptochromesDarknessHEK293 CellsHumansProtein MultimerizationProtein Structure, QuaternaryCryptochromescryptochromelight signalingoligomerizationphotomorphogenesis

Identifiers

PMID31953223
PMCPMC7056577
OpenAlexW3000184544

What OpenQuestion holds

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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.