Evidence map›Paper›PMID 27101846›Full record

ArticleDisease models & mechanisms2016

A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defects.

Simona Langellotti, Valentina Romano, Giulia Romano, Raffaella Klima, Fabian Feiguin, Lucia Cragnaz, Maurizio Romano, Francisco E Baralle

Open access · goldAbstract read
In one paragraph

Article in Disease models & mechanisms, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Loss of TDP-43 Drives Innate Immune Activation Through Relish inInternational journal of molecular sciences · 2026
    Article
  2. Article
  3. Review
  4. A Novel Drosophila-based Drug Repurposing Platform Identified Fingolimod As a Potential Therapeutic for TDP-43 Proteinopathy.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2023
    Article
  5. Article
  6. Article
  7. Where and Why Modeling Amyotrophic Lateral Sclerosis.International journal of molecular sciences · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. 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 2 institutions in 1 country.

Simona LangellottiInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste I-34149, Italy.ORCID 0000-0001-6535-1133
Valentina RomanoInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste I-34149, Italy.ORCID 0000-0002-4820-2897
Giulia RomanoInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste I-34149, Italy.
Raffaella KlimaInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste I-34149, Italy.
Fabian FeiguinInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste I-34149, Italy.
Lucia CragnazInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste I-34149, Italy.
Maurizio RomanoDepartment of Life Sciences, University of Trieste, Via A. Valerio 28, Trieste 34127, Italy mromano@units.it baralle@icgeb.org.
Francisco E BaralleInternational Centre for Genetic Engineering and Biotechnology, Padriciano 99, Trieste I-34149, Italy mromano@units.it baralle@icgeb.org.ORCID 0000-0002-4645-2809
International Centre for Genetic Engineering and Biotechnology · ITUniversity of Trieste · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transactive response DNA-binding protein 43 kDa (TDP-43, also known as TBPH in Drosophila melanogaster and TARDBP in mammals) is the main protein component of the pathological inclusions observed in neurons of patients affected by different neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration (FTLD). The number of studies investigating the molecular mechanisms underlying neurodegeneration is constantly growing; however, the role played by TDP-43 in disease onset and progression is still unclear. A fundamental shortcoming that hampers progress is the lack of animal models showing aggregation of TDP-43 without overexpression. In this manuscript, we have extended our cellular model of aggregation to a transgenic Drosophila line. Our fly model is not based on the overexpression of a wild-type TDP-43 transgene. By contrast, we engineered a construct that includes only the specific TDP-43 amino acid sequences necessary to trigger aggregate formation and capable of trapping endogenous Drosophila TDP-43 into a non-functional insoluble form. Importantly, the resulting recombinant product lacks functional RNA recognition motifs (RRMs) and, thus, does not have specific TDP-43-physiological functions (i.e. splicing regulation ability) that might affect the animal phenotype per se. This novel Drosophila model exhibits an evident degenerative phenotype with reduced lifespan and early locomotion defects. Additionally, we show that important proteins involved in neuromuscular junction function, such as syntaxin (SYX), decrease their levels as a consequence of TDP-43 loss of function implying that the degenerative phenotype is a consequence of TDP-43 sequestration into the aggregates. Our data lend further support to the role of TDP-43 loss-of-function in the pathogenesis of neurodegenerative disorders. The novel transgenic Drosophila model presented in this study will help to gain further insight into the molecular mechanisms underlying neurodegeneration and will provide a valuable system to test potential therapeutic agents to counteract disease.

Indexed as

LocomotionAnimalsBiological AssayDisease Models, AnimalDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsFluorescent Antibody TechniqueGene Expression RegulationHEK293 CellsHumansLarvaNeuromuscular JunctionNeuronsPresynaptic TerminalsProtein AggregatesDNA-Binding ProteinsDrosophila ProteinsProtein AggregatesTBPH protein, DrosophilaAggregationALSDrosophilaFTLDN-terminusTBPHTDP-43

Identifiers

PMID27101846
PMCPMC4920146
OpenAlexW2340331243

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.