Evidence map›Paper›PMID 24113842›Full record

ArticleMolecular neurobiology2013

TDP-43 regulates the microprocessor complex activity during in vitro neuronal differentiation.

Valerio Di Carlo, Elena Grossi, Pietro Laneve, Mariangela Morlando, Stefano Dini Modigliani, Monica Ballarino, Irene Bozzoni, Elisa Caffarelli

Abstract read
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In one paragraph

Article in Molecular neurobiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

39 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Review
  3. Regulatory role of RNA-binding proteins in microRNA biogenesis.Frontiers in molecular biosciences · 2024
    Review
  4. Article
  5. Review
  6. Systems Biology to Address Unmet Medical Needs in Neurological Disorders.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  7. Modulation of miRISC-Mediated Gene Silencing in Eukaryotes.Frontiers in molecular biosciences · 2022
    Review
  8. Article
  9. Review
  10. Protein Aggregation in the Pathogenesis of Ischemic Stroke.Cellular and molecular neurobiology · 2021
    Review
  11. Article
  12. Trends in Understanding the Pathological Roles of TDP-43 and FUS Proteins.Advances in experimental medicine and biology · 2021
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

8 authors at 3 institutions in 1 country.

Valerio Di CarloDepartment of Biology and Biotechnology Charles Darwin, Sapienza University of Rome, P.le A. Moro 5, 00185, Rome, Italy.
Elena Grossi
Pietro Laneve
Mariangela Morlando
Stefano Dini Modigliani
Monica Ballarino
Irene Bozzoni
Elisa Caffarelli
Sapienza University of Rome · ITInstitute of Molecular Biology and Pathology · ITItalian Institute of Technology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TDP-43 (TAR DNA-binding protein 43) is an RNA-binding protein implicated in RNA metabolism at several levels. Even if ubiquitously expressed, it is considered as a neuronal activity-responsive factor and a major signature for neurological pathologies, making the comprehension of its activity in the nervous system a very challenging issue. TDP-43 has also been described as an accessory component of the Drosha-DGCR8 (DiGeorge syndrome critical region gene 8) microprocessor complex, which is crucially involved in basal and tissue-specific RNA processing events. In the present study, we exploited in vitro neuronal differentiation systems to investigate the TDP-43 demand for the microprocessor function, focusing on both its canonical microRNA biosynthetic activity and its alternative role as a post-transcriptional regulator of gene expression. Our findings reveal a novel role for TDP-43 as an essential factor that controls the stability of Drosha protein during neuronal differentiation, thus globally affecting the production of microRNAs. We also demonstrate that TDP-43 is required for the Drosha-mediated regulation of Neurogenin 2, a master gene orchestrating neurogenesis, whereas post-transcriptional control of Dgcr8, another Drosha target, resulted to be TDP-43-independent. These results implicate a previously uncovered contribution of TDP-43 in regulating the abundance and the substrate specificity of the microprocessor complex and provide new insights into TDP-43 as a key player in neuronal differentiation.

Indexed as

Basic Helix-Loop-Helix ProteinsCell DifferentiationCell Line, TumorDNA-Binding ProteinsGene Expression ProfilingGene Expression Regulation, NeoplasticGene Knockdown TechniquesHumansMicroRNAsModels, BiologicalNerve Tissue ProteinsNeuroblastomaNeuronsProteasome InhibitorsProtein BindingProteinsBasic Helix-Loop-Helix ProteinsDGCR8 protein, humanDNA-Binding ProteinsDROSHA protein, humanMicroRNAsNerve Tissue ProteinsNEUROG2 protein, humanProteasome InhibitorsProteinsRibonuclease IIIRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID24113842
OpenAlexW2062902511

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.