Evidence map›Paper›PMID 33524550›Full record

ArticleMolecular plant2021

Light-stabilized FHA2 suppresses miRNA biogenesis through interactions with DCL1 and HYL1.

Seung Jun Park, Suk Won Choi, Gu Min Kim, Christian Møller, Hyun-Sook Pai, Seong Wook Yang

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Molecular plant, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.0field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

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  10. Proceedings of the National Academy of Sciences of the United States of America · 2022
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  11. Review
  12. Article
  13. HYL1-CLEAVAGE SUBTILASE 1 (HCS1) suppresses miRNA biogenesis in response to light-to-dark transition.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. InFrontiers in plant science · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Seung Jun ParkDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Suk Won ChoiDepartment of Systems Biology, Institute of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Gu Min KimDepartment of Systems Biology, Institute of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Christian MøllerDepartment of Systems Biology, Institute of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Hyun-Sook PaiDepartment of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea. Electronic address: hspai@yonsei.ac.kr.
Seong Wook YangDepartment of Systems Biology, Institute of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea; Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg, Copenhagen, Denmark; Pohang University of Science and Technology (POSTECH), 77 Cheongam-Ro, Nam-Gu, Pohang, Gyeongbuk, 37673, Korea. Electronic address: yangsw@yonsei.ac.kr.
Yonsei University · KRPohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The precise regulation of microRNA (miRNA) biogenesis is crucial for plant development, which requires core microprocessors and many fine tuners to coordinate their miRNA processing activity/specificity in fluctuating cellular environments. During de-etiolation, light triggers a dramatic accumulation of core microprocessors and primary miRNAs (pri-miRNAs) but decreases pri-miRNA processing activity, resulting in relatively constant miRNA levels. The mechanisms underlying these seemingly contradictory regulatory changes remain unclear. In this study, we identified forkhead-associated domain 2 (FHA2) as a light-stabilized suppressor of miRNA biogenesis. We found that FHA2 deficiency increased the level of mature miRNAs, accompanied by a reduction in pri-miRNAs and target mRNAs. Biochemical assays showed that FHA2 associates with the core microprocessors DCL1, HYL1, and SE, forming a complex to suppress their pri-miRNA processing activity. Further analyses revealed that FHA2 promotes HYL1 binding but inhibits the binding of DCL1-PAZ-RNase-RNA-binding domains (DCL1-PRR) to miRNAs, whereas FHA2 does not directly bind to these RNAs. Interestingly, we found that FHA2 protein is unstable in the dark but stabilized by light during de-etiolation. Consistently, disruption of FHA led to defects in light-triggered changes in miRNA expression and reduced the survival rate of de-etiolated seedlings after prolonged light deprivation. Collectively, these data suggest that FHA2 is a novel light-stabilized suppressor of miRNA biogenesis and plays a role in fine-tuning miRNA processing during de-etiolation.

Indexed as

LightArabidopsis ProteinsCell Cycle ProteinsMicroRNAsNuclear ProteinsRibonuclease IIIRNA-Binding ProteinsArabidopsis ProteinsCell Cycle ProteinsDCL1 protein, ArabidopsisFHA2 protein, ArabidopsisHYL1 protein, ArabidopsisMicroRNAsNuclear ProteinsRibonuclease IIIRNA-Binding ProteinsmiRNA biogenesismiRNA-biogenetic inconsistencySuppressor of the microprocessor

Identifiers

PMID33524550
OpenAlexW3126542171

What OpenQuestion holds

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Registered trials

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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.