Evidence map›Paper›PMID 35484296›Full record

ArticleScientific reports2022

An Arabidopsis mutant deficient in phosphatidylinositol-4-phosphate kinases ß1 and ß2 displays altered auxin-related responses in roots.

Anastasiia Starodubtseva, Tetiana Kalachova, Katarzyna Retzer, Adriana Jelínková, Petre Dobrev, Jozef Lacek, Romana Pospíchalová, Jindřiška Angelini, Anne Guivarc'h, Stéphanie Pateyron and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Regulation of PIN-FORMED Protein Degradation.International journal of molecular sciences · 2023
    Review
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

13 authors at 7 institutions in 2 countries.

Anastasiia StarodubtsevaInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic.
Tetiana KalachovaInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic. kalachova@ueb.cas.cz.
Katarzyna RetzerInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic.
Adriana JelínkováInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic.
Petre DobrevInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic.
Jozef LacekInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic.
Romana PospíchalováInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic.
Jindřiška AngeliniUniversity of Chemistry and Technology, Technická 5, 16628, Prague, Czech Republic.
Anne Guivarc'hSorbonne Université, UPEC, CNRS, IRD, INRAE, Institute of Ecology and Environmental Sciences of Paris (iEES), 75005, Paris, France.
Stéphanie PateyronUniversité de Paris, CNRS, INRAE, Institute of Plant Sciences Paris-Saclay (IPS2), 91405, Orsay, France.
Ludivine Soubigou-TaconnatUniversité de Paris, CNRS, INRAE, Institute of Plant Sciences Paris-Saclay (IPS2), 91405, Orsay, France.
Lenka BurketováInstitute of Experimental Botany of the Czech Academy of Sciences, Rozvojová 263, 165 02, Prague, Czech Republic.
Eric RuellandUniversité de Technologie de Compiègne, Enzyme and Cell Engineering Laboratory, CNRS, 60203, Compiègne, France.
Czech Academy of Sciences, Institute of Experimental Botany · CZCentre National de la Recherche Scientifique · FRInstitut des Sciences des Plantes de Paris Saclay · FRInstitut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRSorbonne Université · FRUniversité de Technologie de Compiègne · FRUniversity of Chemistry and Technology, Prague · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphatidylinositol 4-kinases (PI4Ks) are the first enzymes that commit phosphatidylinositol into the phosphoinositide pathway. Here, we show that Arabidopsis thaliana seedlings deficient in PI4Kβ1 and β2 have several developmental defects including shorter roots and unfinished cytokinesis. The pi4kβ1β2 double mutant was insensitive to exogenous auxin concerning inhibition of root length and cell elongation; it also responded more slowly to gravistimulation. The pi4kß1ß2 root transcriptome displayed some similarities to a wild type plant response to auxin. Yet, not all the genes displayed such a constitutive auxin-like response. Besides, most assessed genes did not respond to exogenous auxin. This is consistent with data with the transcriptional reporter DR5-GUS. The content of bioactive auxin in the pi4kß1ß2 roots was similar to that in wild-type ones. Yet, an enhanced auxin-conjugating activity was detected and the auxin level reporter DII-VENUS did not respond to exogenous auxin in pi4kß1ß2 mutant. The mutant exhibited altered subcellular trafficking behavior including the trapping of PIN-FORMED 2 protein in rapidly moving vesicles. Bigger and less fragmented vacuoles were observed in pi4kß1ß2 roots when compared to the wild type. Furthermore, the actin filament web of the pi4kß1ß2 double mutant was less dense than in wild-type seedling roots, and less prone to rebuilding after treatment with latrunculin B. A mechanistic model is proposed in which an altered PI4K activity leads to actin filament disorganization, changes in vesicle trafficking, and altered auxin homeostasis and response resulting in a pleiotropic root phenotypes.

Indexed as

ArabidopsisArabidopsis ProteinsIndoleacetic AcidsPhosphatidylinositol PhosphatesPhosphatidylinositolsPlant RootsArabidopsis ProteinsIndoleacetic Acidsphosphatidylinositol 4-phosphatePhosphatidylinositol PhosphatesPhosphatidylinositols

Identifiers

PMID35484296
PMCPMC9051118
OpenAlexW4225010616

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.