Evidence map›Paper›PMID 24794527›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Plastidial transporters KEA1, -2, and -3 are essential for chloroplast osmoregulation, integrity, and pH regulation in Arabidopsis.

Hans-Henning Kunz, Markus Gierth, Andrei Herdean, Mio Satoh-Cruz, David M Kramer, Cornelia Spetea, Julian I Schroeder

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
28.5field-weighted citation impact, top 1% 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

111 citing papers in PubMed, 275 citations in OpenAlex.

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51 more citing papers are in PubMed but not listed here.

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 4 institutions in 3 countries.

Hans-Henning KunzDivision of Biological Sciences, Section of Cell and Developmental Biology, Center for Food and Fuel for the 21st Century, University of California, San Diego, La Jolla, CA 92093-0116;
Markus GierthDepartment of Botany II, University of Cologne, 50674 Cologne, Germany;
Andrei HerdeanDepartment of Biological and Environmental Sciences, University of Gothenburg, 40530 Gothenburg, Sweden; and.
Mio Satoh-CruzDepartment of Energy Plant Research, Michigan State University, East Lansing, MI 48824-1312.
David M KramerDepartment of Energy Plant Research, Michigan State University, East Lansing, MI 48824-1312.
Cornelia SpeteaDepartment of Biological and Environmental Sciences, University of Gothenburg, 40530 Gothenburg, Sweden; and.
Julian I SchroederDivision of Biological Sciences, Section of Cell and Developmental Biology, Center for Food and Fuel for the 21st Century, University of California, San Diego, La Jolla, CA 92093-0116; jischroeder@ucsd.edu.
Michigan State University · USUniversity of California, San Diego · USUniversity of Gothenburg · SEUniversity of Cologne · DE

Funding

Yeast Genetics and Stress Response Genes-BiomedicalP42ES010337 · NIEHS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TUKEY, ROBERT H · 2000 to 2022
$69.8M
NIEHS NIH HHS P42 ES010337NIEHS NIH HHS P42ES010337
6 · The paper itself

Abstract

Multiple K(+) transporters and channels and the corresponding mutants have been described and studied in the plasma membrane and organelle membranes of plant cells. However, knowledge about the molecular identity of chloroplast K(+) transporters is limited. Potassium transport and a well-balanced K(+) homeostasis were suggested to play important roles in chloroplast function. Because no loss-of-function mutants have been identified, the importance of K(+) transporters for chloroplast function and photosynthesis remains to be determined. Here, we report single and higher-order loss-of-function mutants in members of the cation/proton antiporters-2 antiporter superfamily KEA1, KEA2, and KEA3. KEA1 and KEA2 proteins are targeted to the inner envelope membrane of chloroplasts, whereas KEA3 is targeted to the thylakoid membrane. Higher-order but not single mutants showed increasingly impaired photosynthesis along with pale green leaves and severely stunted growth. The pH component of the proton motive force across the thylakoid membrane was significantly decreased in the kea1kea2 mutants, but increased in the kea3 mutant, indicating an altered chloroplast pH homeostasis. Electron microscopy of kea1kea2 leaf cells revealed dramatically swollen chloroplasts with disrupted envelope membranes and reduced thylakoid membrane density. Unexpectedly, exogenous NaCl application reversed the observed phenotypes. Furthermore, the kea1kea2 background enables genetic analyses of the functional significance of other chloroplast transporters as exemplified here in kea1kea2Na(+)/H(+) antiporter1 (nhd1) triple mutants. Taken together, the presented data demonstrate a fundamental role of inner envelope KEA1 and KEA2 and thylakoid KEA3 transporters in chloroplast osmoregulation, integrity, and ion and pH homeostasis.

Indexed as

OsmoregulationArabidopsisArabidopsis ProteinsChloroplastsGene Expression Regulation, PlantHomeostasisHydrogen-Ion ConcentrationIonsMutationPhenotypePhotosynthesisPlant LeavesPlastidsPotassiumPotassium-Hydrogen AntiportersThylakoidsArabidopsis ProteinsIonsKEA1 protein, ArabidopsisKEA3 protein, ArabidopsisPotassiumPotassium-Hydrogen Antiporterspotassium transporter, Arabidopsis

Identifiers

PMID24794527
PMCPMC4034250
OpenAlexW1974627990

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.