Evidence map›Paper›PMID 38438476›Full record

ArticleCommunications biology2024

Regulation of developmental gatekeeping and cell fate transition by the calpain protease DEK1 in Physcomitrium patens.

Viktor Demko, Tatiana Belova, Maxim Messerer, Torgeir R Hvidsten, Pierre-François Perroud, Ako Eugene Ako, Wenche Johansen, Klaus F X Mayer, Odd-Arne Olsen, Daniel Lang

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Leaf Morphogenesis: Insights From the MossFrontiers in plant science · 2021
    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

10 authors at 6 institutions in 5 countries.

Viktor DemkoDepartment of Plant Sciences, Norwegian University of Life Sciences, P.O. Box 5003, NO-1432, Ås, Norway.
Tatiana BelovaDepartment of Plant Sciences, Norwegian University of Life Sciences, P.O. Box 5003, NO-1432, Ås, Norway.
Maxim MessererPlant Genome and Systems Biology, Helmholtz Center Munich-Research Center for Environmental Health, 85764, Neuherberg, Germany.ORCID 0000-0003-0554-5045
Torgeir R HvidstenFaculty of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.ORCID 0000-0001-6097-2539
Pierre-François PerroudInstitut Jean-Pierre Bourgin, INRAE, AgroParisTech, Université Paris-Saclay, 78000, Versailles, France.ORCID 0000-0001-7607-3618
Ako Eugene AkoDepartment of Biotechnology, Inland Norway University of Applied Sciences, Holsetgata 31, 2318, Hamar, Norway.
Wenche JohansenDepartment of Biotechnology, Inland Norway University of Applied Sciences, Holsetgata 31, 2318, Hamar, Norway.
Klaus F X MayerPlant Genome and Systems Biology, Helmholtz Center Munich-Research Center for Environmental Health, 85764, Neuherberg, Germany.
Odd-Arne OlsenDepartment of Plant Sciences, Norwegian University of Life Sciences, P.O. Box 5003, NO-1432, Ås, Norway.ORCID 0000-0002-8787-1057
Daniel LangPlant Genome and Systems Biology, Helmholtz Center Munich-Research Center for Environmental Health, 85764, Neuherberg, Germany. daniel.lang@mailbox.org.ORCID 0000-0002-2166-0716
Helmholtz Zentrum München · DENorwegian University of Life Sciences · NOUniversity of Inland Norway · NOAgroParisTech · FRInstitute of Chemistry of the Slovak Academy of Sciences · SKUniversity of Oslo · NO

Funding

Agentúra na Podporu Výskumu a Vývoja (Slovak Research and Development Agency) APVV-17-0570Agentúra na Podporu Výskumu a Vývoja (Slovak Research and Development Agency) APVV-21-0227Norges Forskningsråd (Research Council of Norway) FRIMEDBIO grant 240343
6 · The paper itself

Abstract

Calpains are cysteine proteases that control cell fate transitions whose loss of function causes severe, pleiotropic phenotypes in eukaryotes. Although mainly considered as modulatory proteases, human calpain targets are directed to the N-end rule degradation pathway. Several such targets are transcription factors, hinting at a gene-regulatory role. Here, we analyze the gene-regulatory networks of the moss Physcomitrium patens and characterize the regulons that are misregulated in mutants of the calpain DEFECTIVE KERNEL1 (DEK1). Predicted cleavage patterns of the regulatory hierarchies in five DEK1-controlled subnetworks are consistent with a pleiotropic and regulatory role during cell fate transitions targeting multiple functions. Network structure suggests DEK1-gated sequential transitions between cell fates in 2D-to-3D development. Our method combines comprehensive phenotyping, transcriptomics and data science to dissect phenotypic traits, and our model explains the protease function as a switch gatekeeping cell fate transitions potentially also beyond plant development.

Indexed as

BryopsidaPeptide HydrolasesCalpainCell DifferentiationEndopeptidasesHumansCalpainEndopeptidasesPeptide Hydrolases

Identifiers

PMID38438476
PMCPMC10912778
OpenAlexW4392371607

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.