Evidence map›Paper›PMID 35332238›Full record

ArticleScientific reports2022

Transport efficiency of AtGTR1 dependents on the hydrophobicity of transported glucosinolates.

Yi-Chia Chung, Hao-Yu Cheng, Wei-Tung Wang, Yen-Jui Chang, Shih-Ming Lin

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Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

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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

5 citing papers in PubMed, 11 citations in OpenAlex.

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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

5 authors at 1 institution in 1 country.

Yi-Chia ChungDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.
Hao-Yu ChengDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.
Wei-Tung WangDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.
Yen-Jui ChangDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan.
Shih-Ming LinDepartment of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, Taiwan. smlin@mail.ncku.edu.tw.
National Cheng Kung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucosinolates (GLSs) are a group of secondary metabolites that are involved in the defense of herbivores. In Arabidopsis thaliana, Glucosinolate Transporter 1 (AtGTR1) transports GLSs with high affinity via a proton gradient-driven process. In addition to transporting GLSs, AtGTR1 also transports phytohormones, jasmonic acid-isoleucine (JA-Ile), and gibberellin (GA). However, little is known about the mechanisms underlying the broad substrate specificity of AtGTR1. Here, we characterized the substrate preference of AtGTR1 by using a yeast uptake assay, and the results revealed that GLS transport rates are negatively correlated with the hydrophobicity of substrates. Interestingly, the AtGTR1 showed a higher substrate affinity for GLSs with higher hydrophobicity, suggesting a hydrophobic substrate binding pocket. In addition, competition assays revealed that JA, salicylic acid (SA), and indole-3-acetic acid (IAA) competed with GLS for transport in yeast, suggesting a potential interaction of AtGTR1 with these phytohormones. To further characterize the functional properties of AtGTR1, mutagenesis experiments confirmed that the conserved EXXEK motif and Arg166 are essential for the GLS transport function. In addition, the purified AtGTR1 adopts a homodimeric conformation, which is possibly regulated by phosphorylation on Thr105. The phosphomimetic mutation, T105D, reduced its protein expression and completely abrogated its GLS transport function, indicating the essential role of phosphorylation on AtGTR1. In summary, this study investigated various factors associated with the GLS transport and increased our knowledge on the substrate preferences of AtGTR1. These findings contribute to understanding how the distribution of defense GLSs is regulated in plants and could be used to improve crop quality in agriculture.

Indexed as

ArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantGlucosinolatesHydrophobic and Hydrophilic InteractionsMembrane Transport ProteinsPlant Growth RegulatorsSaccharomyces cerevisiaeArabidopsis ProteinsGlucosinolatesMembrane Transport ProteinsPlant Growth Regulators

Identifiers

PMID35332238
PMCPMC8948214
OpenAlexW4226267209

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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.