Evidence map›Paper›PMID 19307188›Full record

ArticleThe Journal of biological chemistry2009

Mutants of the Arabidopsis thaliana cation/H+ antiporter AtNHX1 conferring increased salt tolerance in yeast: the endosome/prevacuolar compartment is a target for salt toxicity.

Agustín Hernández, Xingyu Jiang, Beatriz Cubero, Pedro M Nieto, Ray A Bressan, Paul M Hasegawa, José M Pardo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 81 citations in OpenAlex.

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  12. KPlant physiology · 2018
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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

7 authors at 3 institutions in 2 countries.

Agustín HernándezInstituto de Recursos Naturales y Agrobiología, Consejo Superior de Investigaciones Científicas (IRNASE-CSIC), Avda. Reina Mercedes 10, Seville 41012, Spain.
Xingyu Jiang
Beatriz Cubero
Pedro M Nieto
Ray A Bressan
Paul M Hasegawa
José M Pardo
Consejo Superior de Investigaciones Científicas · ESInstituto de Recursos Naturales y Agrobiología de Sevilla · ESPurdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutants of the plant cation/H(+) antiporter AtNHX1 that confer greater halotolerance were generated by random mutagenesis and selected in yeast by phenotypic complementation. The amino acid substitutions that were selected were conservative and occurred in the second half of the membrane-associated N terminus. AtNHX1 complemented the lack of endogenous ScNHX1 in endosomal protein trafficking assays. Growth enhancement on hygromycin B and vanadate media agreed with a generally improved endosomal/prevacuolar function of the mutated proteins. In vivo measurements by (31)P NMR revealed that wild-type and mutant AtNHX1 transporters did not affect cytosolic or vacuolar pH. Surprisingly, when yeast cells were challenged with lithium, a tracer for sodium, the main effect of the mutations in AtNHX1 was a reduction in the amount of compartmentalized lithium. When purified and reconstituted into proteoliposomes or assayed in intact vacuoles isolated from yeast cells, a representative mutant transporter (V318I) showed a greater cation discrimination favoring potassium transport over that of sodium or lithium. Together, our data suggest that the endosome/prevacuolar compartment is a target for salt toxicity. Poisoning by toxic cations in the endosome/prevacuolar compartment is detrimental for cell functions, but it can be alleviated by improving the discrimination of transported alkali cations by the resident cation/H(+) antiporter.

Indexed as

ArabidopsisArabidopsis ProteinsCationsCation Transport ProteinsCell CompartmentationEndosomesGenetic Complementation TestHydrogen-Ion ConcentrationIntracellular SpaceMagnetic Resonance SpectroscopyModels, BiologicalMutationPhenotypeProtein TransportProteolipidsSaccharomyces cerevisiaeArabidopsis ProteinsCationsCation Transport ProteinsNHX1 protein, ArabidopsisProteolipidsproteoliposomesSodium ChlorideSodium-Hydrogen Exchangers

Identifiers

PMID19307188
PMCPMC2682876
OpenAlexW2142592897

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.