Evidence map›Paper›PMID 25103875›Full record

ArticleThe New phytologist2014

Identification and functional assay of the interaction motifs in the partner protein OsNAR2.1 of the two-component system for high-affinity nitrate transport.

Xiaoqin Liu, Daimin Huang, Jinyuan Tao, Anthony J Miller, Xiaorong Fan, Guohua Xu

Open access · hybridAbstract read
In one paragraph

Article in The New phytologist, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  8. OsNLP3 and OsPHR2 orchestrate direct and mycorrhizal pathways for nitrate uptake by regulating NAR2.1-NRT2s complexes in rice.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
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  14. Frontiers in plant science · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Molecular Regulatory Networks for Improving Nitrogen Use Efficiency in Rice.International journal of molecular sciences · 2021
    Review
  19. Proofing Direct-Seeded Rice with Better Root Plasticity and Architecture.International journal of molecular sciences · 2021
    Review
  20. Article
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 2 institutions in 2 countries.

Xiaoqin LiuState Key Laboratory of Crop Genetics and Germplasm Enhancement, Nanjing Agricultural University, Nanjing, 210095, China.
Daimin HuangMOA Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Nanjing Agricultural University, Nanjing, 210095, China.
Jinyuan TaoMOA Key Laboratory of Plant Nutrition and Fertilization in Low-Middle Reaches of the Yangtze River, Nanjing Agricultural University, Nanjing, 210095, China.
Anthony J MillerMetabolic Biology Department, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, UK.
Xiaorong FanState Key Laboratory of Crop Genetics and Germplasm Enhancement, Nanjing Agricultural University, Nanjing, 210095, China.
Guohua XuState Key Laboratory of Crop Genetics and Germplasm Enhancement, Nanjing Agricultural University, Nanjing, 210095, China.
Nanjing Agricultural University · CNNorwich Research Park · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J004561/1
6 · The paper itself

Abstract

A partner protein, NAR2, is essential for high-affinity nitrate transport of the NRT2 protein in plants. However, the NAR2 motifs that interact with NRT2s for their plasma membrane (PM) localization and nitrate transporter activity have not been functionally characterized. In this study, OsNAR2.1 mutations with different carbon (C)-terminal deletions and nine different point mutations in the conserved regions of NAR2 homologs in plants were generated to explore the essential motifs involved in the interaction with OsNRT2.3a. Screening using the membrane yeast two-hybrid system and Xenopus oocytes for nitrogen-15 ((15)N) uptake demonstrated that either R100G or D109N point mutations impaired the OsNAR2.1 interaction with OsNRT2.3a. Western blotting and visualization using green fluorescent protein fused to either the N- or C-terminus of OsNAR2.1 indicated that OsNAR2.1 is expressed in both the PM and cytoplasm. The split-yellow fluorescent protein (YFP)/BiFC analyses indicated that OsNRT2.3a was targeted to the PM in the presence of OsNAR2.1, while either R100G or D109N mutation resulted in the loss of OsNRT2.3a-YFP signal in the PM. Based on these results, arginine 100 and aspartic acid 109 of the OsNAR2.1 protein are key amino acids in the interaction with OsNRT2.3a, and their interaction occurs in the PM but not cytoplasm.

Indexed as

AnimalsAnion Transport ProteinsArginineBiological TransportCell MembraneCytoplasmGreen Fluorescent ProteinsNitratesNitrate TransportersOocytesOryzaPlant ProteinsPoint MutationProtein Interaction Domains and MotifsTwo-Hybrid System TechniquesXenopusAnion Transport ProteinsArginineGreen Fluorescent ProteinsNitratesNitrate TransportersPlant Proteinshigh-affinity transport system two-component transporterinteraction motifsNAR2.1NRT2.3aOryza sativa

Identifiers

PMID25103875
PMCPMC4232926
OpenAlexW2022482441

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.