Evidence map›Paper›PMID 34463721›Full record

ArticleThe Plant cell2021

Light-Response Bric-A-Brack/Tramtrack/Broad proteins mediate cryptochrome 2 degradation in response to low ambient temperature.

Libang Ma, Xu Li, Zhiwei Zhao, Yuhao Hao, Ruixin Shang, Desheng Zeng, Hongtao Liu

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Molecular regulatory mechanisms ofForestry research · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Signaling Mechanisms by Arabidopsis Cryptochromes.Frontiers in plant science · 2022
    Review
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Libang MaNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.ORCID 0000-0002-1044-2000
Xu LiNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.ORCID 0000-0002-8835-3630
Zhiwei ZhaoNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.ORCID 0000-0001-5624-3886
Yuhao HaoNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.ORCID 0000-0002-1426-8978
Ruixin ShangNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.ORCID 0000-0001-9052-9052
Desheng ZengNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.ORCID 0000-0003-0001-3242
Hongtao LiuNational Key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai 200032, China.ORCID 0000-0002-6363-7450
Chinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cryptochromes (crys) are photolyase-like blue-light receptors first discovered in Arabidopsis thaliana and later identified in all major evolutionary lineages. Crys are involved in not only blue light responses but also in temperature responses; however, whether and how cry protein stability is regulated by temperature remains unknown. Here, we show that cry2 protein abundance is modulated by ambient temperature and cry2 protein is degraded under low ambient temperature via the 26S proteasome. Consistent with this, cry2 shows high levels of ubiquitination under low ambient temperatures. Interestingly, cry2 degradation at low ambient temperatures occurs only under blue light and not under red light or dark conditions, indicating blue-light-dependent degradation of cry2 at low ambient temperature. Furthermore, low ambient temperature promotes physical interaction of Light-Response Bric-a-Brack/Tramtrack/Broad (LRB) proteins with cry2 to modulate its ubiquitination and protein stability in response to ambient temperature. LRBs promote high-temperature-induced hypocotyl elongation by modulating the protein stability of cry2 protein. These results indicate that cry2 accumulation is regulated by not only blue light but also ambient temperature, and LRBs are responsible for cry2 degradation at low ambient temperature. The stabilization of cry2 by high temperature makes cry2 a better negative regulator of temperature responses.

Indexed as

Cold TemperatureArabidopsisArabidopsis ProteinsCryptochromesProteasome Endopeptidase ComplexArabidopsis ProteinsATP dependent 26S proteaseCRY2 protein, ArabidopsisCryptochromesProteasome Endopeptidase Complex

Identifiers

PMID34463721
PMCPMC8643628
OpenAlexW3198233292

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.