Evidence map›Paper›PMID 32627867›Full record

ArticleThe EMBO journal2020

Trnp1 organizes diverse nuclear membrane-less compartments in neural stem cells.

Miriam Esgleas, Sven Falk, Ignasi Forné, Marc Thiry, Sonia Najas, Sirui Zhang, Aina Mas-Sanchez, Arie Geerlof, Dierk Niessing, Zefeng Wang and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 20 citations in OpenAlex.

  1. Journal of gastrointestinal oncology · 2026
    Article
  2. Article
  3. Review
  4. Indirect neurogenesis in space and time.Nature reviews. Neuroscience · 2024
    Review
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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

12 authors at 5 institutions in 3 countries.

Miriam EsgleasPhysiological Genomics, Biomedical Center (BMC), Ludwig-Maximilians Universitaet Muenchen, Planegg/Munich, Germany.
Sven FalkPhysiological Genomics, Biomedical Center (BMC), Ludwig-Maximilians Universitaet Muenchen, Planegg/Munich, Germany.ORCID 0000-0003-4194-9274
Ignasi FornéProtein Analysis Unit, BioMedical Center (BMC), Ludwig-Maximilians-Universitaet Muenchen, Planegg/Munich, Germany.
Marc ThiryCell and Tissue Biology Unit, GIGA-Neurosciences, University of Liege, C.H.U. Sart Tilman, Liege, Belgium.
Sonia NajasPhysiological Genomics, Biomedical Center (BMC), Ludwig-Maximilians Universitaet Muenchen, Planegg/Munich, Germany.
Sirui ZhangCAS Key Laboratory of Computational Biology, CAS-MPG Partner Institute for Computational Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China.ORCID 0000-0002-1992-3345
Aina Mas-SanchezPhysiological Genomics, Biomedical Center (BMC), Ludwig-Maximilians Universitaet Muenchen, Planegg/Munich, Germany.
Arie GeerlofInstitute of Structural Biology, Helmholtz Zentrum Muenchen, Neuherberg, Germany.
Dierk NiessingGroup Intracellular Transport and RNA Biology at the Institute of Structural Biology, Helmholtz Zentrum Muenchen, Neuherberg, Germany.
Zefeng WangCAS Key Laboratory of Computational Biology, CAS-MPG Partner Institute for Computational Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, Shanghai, China.
Axel ImhofProtein Analysis Unit, BioMedical Center (BMC), Ludwig-Maximilians-Universitaet Muenchen, Planegg/Munich, Germany.ORCID 0000-0003-2993-8249
Magdalena GötzPhysiological Genomics, Biomedical Center (BMC), Ludwig-Maximilians Universitaet Muenchen, Planegg/Munich, Germany.ORCID 0000-0003-1551-9203
Helmholtz Zentrum München · DECenter for Integrated Protein Science Munich · DEShanghai Institute of Nutrition and Health · CNLudwig-Maximilians-Universität München · DEUniversity of Liège · BE

Funding

Advanced ERC 340793German Research FoundationNSFC 31730110
6 · The paper itself

Abstract

TMF1-regulated nuclear protein 1 (Trnp1) has been shown to exert potent roles in neural development affecting neural stem cell self-renewal and brain folding, but its molecular function in the nucleus is still unknown. Here, we show that Trnp1 is a low complexity protein with the capacity to phase separate. Trnp1 interacts with factors located in several nuclear membrane-less organelles, the nucleolus, nuclear speckles, and condensed chromatin. Importantly, Trnp1 co-regulates the architecture and function of these nuclear compartments in vitro and in the developing brain in vivo. Deletion of a highly conserved region in the N-terminal intrinsic disordered region abolishes the capacity of Trnp1 to regulate nucleoli and heterochromatin size, proliferation, and M-phase length; decreases the capacity to phase separate; and abrogates most of Trnp1 protein interactions. Thus, we identified Trnp1 as a novel regulator of several nuclear membrane-less compartments, a function important to maintain cells in a self-renewing proliferative state.

Indexed as

Cell DivisionAnimalsCell Cycle ProteinsCell LineCell NucleolusChromatinDNA-Binding ProteinsFemaleMiceNeural Stem CellsNuclear EnvelopeProtein DomainsCell Cycle ProteinsChromatinDNA-Binding ProteinsTrnp1 protein, mouseheterochromatinmitosisnuclear specklesnucleolusphase-transition

Identifiers

PMID32627867
PMCPMC7429739
OpenAlexW3038922638

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.