Evidence map›Paper›PMID 22307851›Full record

ArticleThe Plant cell2012

Mutations in the Arabidopsis homolog of LST8/GβL, a partner of the target of Rapamycin kinase, impair plant growth, flowering, and metabolic adaptation to long days.

Manon Moreau, Marianne Azzopardi, Gilles Clément, Thomas Dobrenel, Chloé Marchive, Charlotte Renne, Marie-Laure Martin-Magniette, Ludivine Taconnat, Jean-Pierre Renou, Christophe Robaglia and 1 more

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
16.9field-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

124 citing papers in PubMed, 237 citations in OpenAlex.

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  18. Plants (Basel, Switzerland) · 2024
    Article
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64 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

11 authors at 3 institutions in 1 country.

Manon MoreauInstitut Jean-Pierre Bourgin, Unité Mixte de Recherche 1318, Institut National de la Recherche Agronomique AgroParisTech, 78026 Versailles cedex, France.
Marianne Azzopardi
Gilles Clément
Thomas Dobrenel
Chloé Marchive
Charlotte Renne
Marie-Laure Martin-Magniette
Ludivine Taconnat
Jean-Pierre Renou
Christophe Robaglia
Christian Meyer
Institut Jean-Pierre Bourgin · FRUniversité d'Évry Val-d'Essonne · FRAgroParisTech · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conserved Target of Rapamycin (TOR) kinase forms high molecular mass complexes and is a major regulator of cellular adaptations to environmental cues. The Lethal with Sec Thirteen 8/G protein β subunit-like (LST8/GβL) protein is a member of the TOR complexes, and two putative LST8 genes are present in Arabidopsis thaliana, of which only one (LST8-1) is significantly expressed. The Arabidopsis LST8-1 protein is able to complement yeast lst8 mutations and interacts with the TOR kinase. Mutations in the LST8-1 gene resulted in reduced vegetative growth and apical dominance with abnormal development of flowers. Mutant plants were also highly sensitive to long days and accumulated, like TOR RNA interference lines, higher amounts of starch and amino acids, including proline and glutamine, while showing reduced concentrations of inositol and raffinose. Accordingly, transcriptomic and enzymatic analyses revealed a higher expression of genes involved in nitrate assimilation when lst8-1 mutants were shifted to long days. The transcriptome of lst8-1 mutants in long days was found to share similarities with that of a myo-inositol 1 phosphate synthase mutant that is also sensitive to the extension of the light period. It thus appears that the LST8-1 protein has an important role in regulating amino acid accumulation and the synthesis of myo-inositol and raffinose during plant adaptation to long days.

Indexed as

PhotoperiodAcclimatizationAmino AcidsArabidopsisArabidopsis ProteinsFlowersGene Expression Regulation, PlantMetabolomeMutationPhosphatidylinositol 3-KinasesPlants, Genetically ModifiedRNA InterferenceTranscriptomeAmino AcidsArabidopsis ProteinsPhosphatidylinositol 3-KinasesTOR protein, Arabidopsis

Identifiers

PMID22307851
PMCPMC3315227
OpenAlexW2155675049

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.