Evidence map›Paper›PMID 21436382›Full record

ArticlePlant physiology2011

Protein phosphatase 2A B55 and A regulatory subunits interact with nitrate reductase and are essential for nitrate reductase activation.

Behzad Heidari, Polina Matre, Dugassa Nemie-Feyissa, Christian Meyer, Odd Arne Rognli, Simon G Møller, Cathrine Lillo

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In one paragraph

Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
7.4field-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

25 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Hyperosmolarity-induced suppression of group B1 Raf-like protein kinases modulates drought-growth trade-off inProceedings of the National Academy of Sciences of the United States of America · 2024
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  3. Review
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  5. Role of protein phosphatases in the regulation of nitrogen nutrition in plants.Physiology and molecular biology of plants : an international journal of functional plant biology · 2021
    Review
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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.

Behzad HeidariUniversity of Stavanger, Centre for Organelle Research, Faculty of Science and Technology, N-4036 Stavanger, Norway.
Polina Matre
Dugassa Nemie-Feyissa
Christian Meyer
Odd Arne Rognli
Simon G Møller
Cathrine Lillo
Institut Jean-Pierre Bourgin · FRUniversity of Stavanger · NONorwegian University of Life Sciences · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Posttranslational activation of nitrate reductase (NR) in Arabidopsis (Arabidopsis thaliana) and other higher plants is mediated by dephosphorylation at a specific Ser residue in the hinge between the molybdenum cofactor and heme-binding domains. The activation of NR in green leaves takes place after dark/light shifts, and is dependent on photosynthesis. Previous studies using various inhibitors pointed to protein phosphatases sensitive to okadaic acid, including protein phosphatase 2A (PP2A), as candidates for activation of NR. PP2As are heterotrimeric enzymes consisting of a catalytic (C), structural (A), and regulatory (B) subunit. In Arabidopsis there are five, three, and 18 of these subunits, respectively. By using inducible artificial microRNA to simultaneously knock down the three structural subunits we show that PP2A is necessary for NR activation. The structural subunits revealed overlapping functions in the activation process of NR. Bimolecular fluorescence complementation was used to identify PP2A regulatory subunits interacting with NR, and the two B55 subunits were positive. Interactions of NR and B55 were further confirmed by the yeast two-hybrid assay. In Arabidopsis the B55 group consists of the close homologs B55α and B55β. Interestingly, the homozygous double mutant (b55α × b55β) appeared to be lethal, which shows that the B55 group has essential functions that cannot be replaced by other regulatory subunits. Mutants homozygous for mutation in Bβ and heterozygous for mutation in Bα revealed a slower activation rate for NR than wild-type plants, pointing to these subunits as part of a PP2A complex responsible for NR dephosphorylation.

Indexed as

ArabidopsisArabidopsis ProteinsMutationNitrate ReductaseOkadaic AcidPhosphorylationProtein Phosphatase 2Two-Hybrid System TechniquesArabidopsis ProteinsNitrate ReductaseOkadaic AcidProtein Phosphatase 2type 2A protein serine-threonine phosphatase 55 kDa B, Arabidopsis

Identifiers

PMID21436382
PMCPMC3091043
OpenAlexW2083585822

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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.