Evidence map›Paper›PMID 31285503›Full record

ArticleScientific reports2019

Phosphorylation of p23-1 cochaperone by protein kinase CK2 affects root development in Arabidopsis.

Stefano D'Alessandro, Serena Golin, Sofia Zanin, Laura Cendron, Michela Zottini, Maria Ruzzene

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.2field-weighted citation impact, top 15% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Split-YFP-coupled interaction-dependent TurboID identifies new functions of basal cell polarity inProceedings of the National Academy of Sciences of the United States of America · 2025
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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

6 authors at 1 institution in 1 country.

Stefano D'AlessandroDepartment of Biology, University of Padova, Via U. Bassi 58/B, I-35131, Padova, Italy.
Serena GolinDepartment of Biology, University of Padova, Via U. Bassi 58/B, I-35131, Padova, Italy.
Sofia ZaninDepartment of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, I-35131, Padova, Italy.
Laura CendronDepartment of Biology, University of Padova, Via U. Bassi 58/B, I-35131, Padova, Italy.ORCID http://orcid.org/0000-0002-0125-0461
Michela ZottiniDepartment of Biology, University of Padova, Via U. Bassi 58/B, I-35131, Padova, Italy. michela.zottini@unipd.it.
Maria RuzzeneDepartment of Biomedical Sciences, University of Padova, Via U. Bassi 58/B, I-35131, Padova, Italy. maria.ruzzene@unipd.it.
University of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Root growth is a fundamental process in plants and assures nutrient and water uptake required for efficient photosynthesis and metabolism. Postembryonic development of roots is controlled by the functionality of the meristem. Several hormones and signaling molecules regulate the size of the meristem, and among them, auxins play a major role. Protein kinase CK2, along with the chaperone protein HSP90, has been found to be involved in the regulation of auxin transport. Here, we show that p23-1, a cochaperone of HSP90, is phosphorylated by CK2 in Arabidopsis. We identified Ser201 as the major CK2 target site in p23-1 and demonstrated that phosphorylation of this site is necessary for normal root development. Moreover, we shed light on the nature of CK2 in Arabidopsis, showing that the three catalytic isoforms, CK2 αA, αB and αC, are proteins of approximately 40 kDa. Our results increase knowledge of the connection among HSP90, p23-1 and CK2 in Arabidopsis, suggesting the existence of a possible common root development mechanism controlled by these signaling molecules.

Indexed as

ArabidopsisArabidopsis ProteinsCasein Kinase IIGene Expression Regulation, DevelopmentalGene Expression Regulation, PlantIndoleacetic AcidsMolecular ChaperonesMolecular WeightPhosphorylationPlant RootsProtein IsoformsProteomicsSerineArabidopsis ProteinsCasein Kinase IIIndoleacetic AcidsMolecular Chaperonesp23 protein, ArabidopsisProtein IsoformsSerine

Identifiers

PMID31285503
PMCPMC6614504
OpenAlexW2959240145

What OpenQuestion holds

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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.