Evidence map›Paper›PMID 33526703›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

The RING E3 ligase SDIR1 destabilizes EBF1/EBF2 and modulates the ethylene response to ambient temperature fluctuations in

Dongdong Hao, Lian Jin, Xing Wen, Feifei Yu, Qi Xie, Hongwei Guo

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
8.4field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

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  8. International journal of molecular sciences · 2024
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  9. Review
  10. Endoribonuclease DNE1 Promotes Ethylene Response by ModulatingInternational journal of molecular sciences · 2024
    Article
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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

6 authors at 3 institutions in 1 country.

Dongdong HaoInstitute of Plant and Food Science, Department of Biology, Southern University of Science and Technology, 518055 Shenzhen, China.ORCID 0000-0002-9692-3007
Lian JinInstitute of Plant and Food Science, Department of Biology, Southern University of Science and Technology, 518055 Shenzhen, China.ORCID 0000-0001-7067-3807
Xing WenInstitute of Plant and Food Science, Department of Biology, Southern University of Science and Technology, 518055 Shenzhen, China.ORCID 0000-0002-9322-2272
Feifei YuState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, The Innovative Academy of Seed Design, Chinese Academy of Sciences, 100101 Beijing, China.
Qi XieState Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, The Innovative Academy of Seed Design, Chinese Academy of Sciences, 100101 Beijing, China.
Hongwei GuoInstitute of Plant and Food Science, Department of Biology, Southern University of Science and Technology, 518055 Shenzhen, China; guohw@sustech.edu.cn.
Southern University of Science and Technology · CNChinese Academy of Sciences · CNPeking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gaseous phytohormone ethylene mediates numerous aspects of plant growth and development as well as stress responses. The F-box proteins EIN3-binding F-box protein 1 (EBF1) and EBF2 are key components that ubiquitinate and degrade the master transcription factors ethylene insensitive 3 (EIN3) and EIN3-like 1 (EIL1) in the ethylene response pathway. Notably, EBF1 and EBF2 themselves undergo the 26S proteasome-mediated proteolysis induced by ethylene and other stress signals. However, despite their importance, little is known about the mechanisms regulating the degradation of these proteins. Here, we show that a really interesting new gene (RING)-type E3 ligase, salt- and drought-induced ring finger 1 (SDIR1), positively regulates the ethylene response and promotes the accumulation of EIN3. Further analyses indicate that SDIR1 directly interacts with EBF1/EBF2 and targets them for ubiquitination and proteasome-dependent degradation. We show that SDIR1 is required for the fine tuning of the ethylene response to ambient temperature changes by mediating temperature-induced EBF1/EBF2 degradation and EIN3 accumulation. Thus, our work demonstrates that SDIR1 functions as an important modulator of ethylene signaling in response to ambient temperature changes, thereby enabling plant adaptation under fluctuating environmental conditions.

Indexed as

ArabidopsisArabidopsis ProteinsDNA-Binding ProteinsDroughtsEthylenesF-Box ProteinsGene Expression Regulation, PlantPlant Growth RegulatorsPlants, Genetically ModifiedProteasome Endopeptidase ComplexProteolysisSignal TransductionTemperatureTranscription FactorsUbiquitinationUbiquitin-Protein LigasesArabidopsis ProteinsATP dependent 26S proteaseDNA-Binding ProteinsEBF1 protein, ArabidopsisEBF2 protein, ArabidopsisEIN3 protein, ArabidopsisethyleneEthylenesF-Box ProteinsPlant Growth RegulatorsProteasome Endopeptidase ComplexSDIR1 protein, ArabidopsisTranscription FactorsUbiquitin-Protein Ligasesambient temperatureEBF1/EBF2ethyleneSDIR1ubiquitination

Identifiers

PMID33526703
PMCPMC8017691
OpenAlexW3128354657

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.