Evidence map›Paper›PMID 10220464›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases.

R P Bhalerao, K Salchert, L Bakó, L Okrész, L Szabados, T Muranaka, Y Machida, J Schell, C Koncz

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
24.0field-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

80 citing papers in PubMed, 210 citations in OpenAlex.

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  17. SUMOylation represses SnRK1 signaling in Arabidopsis.The Plant journal : for cell and molecular biology · 2016
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20 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

R P BhaleraoMax-Planck Institut für Züchtungsforschung, D-50829 Cologne, Germany.
K Salchert
L Bakó
L Okrész
L Szabados
T Muranaka
Y Machida
J Schell
C Koncz
Institute of Plant Biology · HUHungarian Academy of Sciences · HUNagoya University · JPSumitomo Chemical (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutation of the PRL1 gene, encoding a regulatory WD protein, results in glucose hypersensitivity and derepression of glucose-regulated genes in Arabidopsis. The yeast SNF1 protein kinase, a key regulator of glucose signaling, and Arabidopsis SNF1 homologs AKIN10 and AKIN11, which can complement the Deltasnf1 mutation, were found to interact with an N-terminal domain of the PRL1 protein in the two-hybrid system and in vitro. AKIN10 and AKIN11 suppress the yeast Deltasnf4 mutation and interact with the SNF4p-activating subunit of SNF1. PRL1 and SNF4 bind independently to adjacent C-terminal domains of AKIN10 and AKIN11, and these protein interactions are negatively regulated by glucose in yeast. AKIN10 and AKIN11, purified in fusion with glutathione S-transferase, undergo autophosphorylation and phosphorylate a peptide of sucrose phosphate synthase in vitro. The sucrose phosphate synthase-peptide kinase activity of AKIN complexes detected by immunoprecipitation is stimulated by sucrose in light-grown Arabidopsis plants. In comparison with wild type, the activation level of AKIN immunocomplexes is higher in the prl1 mutant, suggesting that PRL1 is a negative regulator of Arabidopsis SNF1 homologs. This conclusion is supported by the observation that PRL1 is an inhibitor of AKIN10 and AKIN11 in vitro.

Indexed as

Arabidopsis ProteinsGene Expression Regulation, PlantIntracellular Signaling Peptides and ProteinsAmino Acid SequenceArabidopsisCarrier ProteinsGenes, FungalGenes, PlantMolecular Sequence DataMutationNuclear ProteinsPlant ProteinsProtein BindingProtein Serine-Threonine KinasesSequence AlignmentArabidopsis ProteinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsPlant ProteinsPRL1 protein, ArabidopsisPRL1 protein, plantProtein Serine-Threonine KinasesSNF1-related protein kinases

Identifiers

PMID10220464
PMCPMC21862
OpenAlexW2165614749

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.