Evidence map›Paper›PMID 19797057›Full record

ArticleThe Journal of biological chemistry2009

The Arabidopsis ATP-binding cassette protein AtMRP5/AtABCC5 is a high affinity inositol hexakisphosphate transporter involved in guard cell signaling and phytate storage.

Réka Nagy, Hanne Grob, Barbara Weder, Porntip Green, Markus Klein, Annie Frelet-Barrand, Jan K Schjoerring, Charles Brearley, Enrico Martinoia

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 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
12.2field-weighted citation impact, top 2% 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

101 citing papers in PubMed, 202 citations in OpenAlex.

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  18. Antibacterial Activity fromPharmaceutics · 2022
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  19. International journal of molecular sciences · 2022
    Article
  20. Biochemistry · 2022
    Article

41 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

9 authors at 5 institutions in 4 countries.

Réka NagyUniversity of Zurich, Institute of Plant Biology, Zollikerstrasse 107, CH-8008 Zürich, Switzerland. rnagy@botinst.uzh.ch
Hanne Grob
Barbara Weder
Porntip Green
Markus Klein
Annie Frelet-Barrand
Jan K Schjoerring
Charles Brearley
Enrico Martinoia
University of Zurich · CHUniversity of East Anglia · GBPhilip Morris International (Switzerland) · CHPohang University of Science and Technology · KRUniversity of Copenhagen · DK

Funding

Biotechnology and Biological Sciences Research Council BB/C514090/1
6 · The paper itself

Abstract

Arabidopsis possesses a superfamily of ATP-binding cassette (ABC) transporters. Among these, the multidrug resistance-associated protein AtMRP5/AtABCC5 regulates stomatal aperture and controls plasma membrane anion channels of guard cells. Remarkably, despite the prominent role of AtMRP5 in conferring partial drought insensitivity upon Arabidopsis, we know little of the biochemical function of AtMRP5. Our phylogenetic analysis showed that AtMRP5 is closely related to maize MRP4, mutation of which confers a low inositol hexakisphosphate kernel phenotype. We now show that insertion mutants of AtMRP5 display a low inositol hexakisphosphate phenotype in seed tissue and that this phenotype is associated with alterations of mineral cation and phosphate status. By heterologous expression in yeast, we demonstrate that AtMRP5 encodes a specific and high affinity ATP-dependent inositol hexakisphosphate transporter that is sensitive to inhibitors of ABC transporters. Moreover, complementation of the mrp5-1 insertion mutants of Arabidopsis with the AtMRP5 cDNA driven from a guard cell-specific promoter restores the sensitivity of the mutant to abscisic acid-mediated inhibition of stomatal opening. Additionally, we show that mutation of residues of the Walker B motif prevents restoring the multiple phenotypes associated with mrp5-1. Our findings highlight a novel function of plant ABC transporters that may be relevant to other kingdoms. They also extend the signaling repertoire of this ubiquitous inositol polyphosphate signaling molecule.

Indexed as

Adenylyl ImidodiphosphateArabidopsis ProteinsATP-Binding Cassette, Sub-Family C ProteinsBiological TransportGenetic Complementation TestGreen Fluorescent ProteinsInositol PhosphatesMicroscopy, ConfocalMicrosomesMutationPhosphorusPhytic AcidPlant EpidermisPlants, Genetically ModifiedPlant StomataSeedsAdenylyl ImidodiphosphateArabidopsis ProteinsATMRP5 protein, ArabidopsisATP-Binding Cassette, Sub-Family C ProteinsGreen Fluorescent ProteinsInositol PhosphatesPhosphorusPhytic Acid

Identifiers

PMID19797057
PMCPMC2785203
OpenAlexW2084632633

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.