Evidence map›Paper›PMID 34919703›Full record

ArticleThe Plant cell2022

Oxylipin signaling in salt-stressed soybean is modulated by ligand-dependent interaction of Class II acyl-CoA-binding proteins with lipoxygenase.

Shiu-Cheung Lung, Sze Han Lai, Haiyang Wang, Xiuying Zhang, Ailin Liu, Ze-Hua Guo, Hon-Ming Lam, Mee-Len Chye

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
6.4field-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

12 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Interaction of Soybean (Plants (Basel, Switzerland) · 2024
    Article
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  6. Article
  7. 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

8 authors at 2 institutions in 1 country.

Shiu-Cheung LungSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.ORCID 0000-0002-6433-4988
Sze Han LaiSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.ORCID 0000-0001-5728-5156
Haiyang WangSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.ORCID 0000-0001-6455-0907
Xiuying ZhangSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.ORCID 0000-0002-5874-6214
Ailin LiuSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.ORCID 0000-0003-4719-8440
Ze-Hua GuoSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.ORCID 0000-0002-7894-498X
Hon-Ming LamSchool of Life Sciences and Centre for Soybean Research of the State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, Hong Kong, China.ORCID 0000-0002-6673-8740
Mee-Len ChyeSchool of Biological Sciences, The University of Hong Kong, Pokfulam, Hong Kong, China.ORCID 0000-0003-3505-3674
University of Hong Kong · HKChinese University of Hong Kong · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant lipoxygenases (LOXs) oxygenate linoleic and linolenic acids, creating hydroperoxy derivatives, and from these, jasmonates and other oxylipins are derived. Despite the importance of oxylipin signaling, its activation mechanism remains largely unknown. Here, we show that soybean ACYL-COA-BINDING PROTEIN3 (ACBP3) and ACBP4, two Class II acyl-CoA-binding proteins, suppressed activity of the vegetative LOX homolog VLXB by sequestering it at the endoplasmic reticulum. The ACBP4-VLXB interaction was facilitated by linoleoyl-CoA and linolenoyl-CoA, which competed with phosphatidic acid (PA) for ACBP4 binding. In salt-stressed roots, alternative splicing produced ACBP variants incapable of VLXB interaction. Overexpression of the variants enhanced LOX activity and salt tolerance in Arabidopsis and soybean hairy roots, whereas overexpressors of the native forms exhibited reciprocal phenotypes. Consistently, the differential alternative splicing pattern in two soybean genotypes coincided with their difference in salt-induced lipid peroxidation. Salt-treated soybean roots were enriched in C32:0-PA species that showed high affinity to Class II ACBPs. We conclude that PA signaling and alternative splicing suppress ligand-dependent interaction of Class II ACBPs with VLXB, thereby triggering lipid peroxidation during salt stress. Hence, our findings unveil a dual mechanism that initiates the onset of oxylipin signaling in the salinity response.

Indexed as

ArabidopsisArabidopsis ProteinsCarrier ProteinsDiazepam Binding InhibitorGlycine maxLigandsLipoxygenaseOxylipinsPhosphatidic AcidsSalt StressACBP3 protein, ArabidopsisArabidopsis ProteinsCarrier ProteinsDiazepam Binding InhibitorLigandsLipoxygenaseOxylipinsPhosphatidic Acids

Identifiers

PMID34919703
PMCPMC8894927
OpenAlexW4200330146

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.