Evidence map›Paper›PMID 33824334›Full record

ArticleNature communications2021

Drosophila TNFRs Grindelwald and Wengen bind Eiger with different affinities and promote distinct cellular functions.

Valentina Palmerini, Silvia Monzani, Quentin Laurichesse, Rihab Loudhaief, Sara Mari, Valentina Cecatiello, Vincent Olieric, Sebastiano Pasqualato, Julien Colombani, Ditte S Andersen and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

22 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Adipocyte-DerivedBiomolecules · 2025
    Article
  7. Glial-derived TNF/Eiger signaling promotes somatosensory neurite sculpting.Cellular and molecular life sciences : CMLS · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Regulating metabolism to shape immune function: Lessons from Drosophila.Seminars in cell & developmental biology · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. International journal of molecular sciences · 2022
    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

11 authors at 3 institutions in 3 countries.

Valentina PalmeriniIEO, European Institute of Oncology IRCCS, Milan, Italy.
Silvia MonzaniIEO, European Institute of Oncology IRCCS, Milan, Italy.
Quentin LaurichesseDepartment of Biology, Faculty of Science, University of Copenhagen, Copenhagen O, Denmark.
Rihab LoudhaiefDepartment of Biology, Faculty of Science, University of Copenhagen, Copenhagen O, Denmark.
Sara MariIEO, European Institute of Oncology IRCCS, Milan, Italy.
Valentina CecatielloIEO, European Institute of Oncology IRCCS, Milan, Italy.
Vincent OliericPaul Scherrer Institute, Villigen-PSI, Switzerland.ORCID 0000-0002-0533-7222
Sebastiano Pasqualato *IEO, European Institute of Oncology IRCCS, Milan, Italy. sebastiano.pasqualato@ieo.it.ORCID 0000-0002-9038-7768
Julien Colombani *Department of Biology, Faculty of Science, University of Copenhagen, Copenhagen O, Denmark. julien.colombani@bio.ku.dk.ORCID 0000-0002-8250-4899
Ditte S Andersen *Department of Biology, Faculty of Science, University of Copenhagen, Copenhagen O, Denmark. ditte.andersen@bio.ku.dk.
Marina Mapelli *IEO, European Institute of Oncology IRCCS, Milan, Italy. marina.mapelli@ieo.it.ORCID 0000-0001-8502-0649
European Institute of Oncology · ITUniversity of Copenhagen · DKPaul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Drosophila tumour necrosis factor (TNF) ligand-receptor system consists of a unique ligand, Eiger (Egr), and two receptors, Grindelwald (Grnd) and Wengen (Wgn), and therefore provides a simple system for exploring the interplay between ligand and receptors, and the requirement for Grnd and Wgn in TNF/Egr-mediated processes. Here, we report the crystallographic structure of the extracellular domain (ECD) of Grnd in complex with Egr, a high-affinity hetero-hexameric assembly reminiscent of human TNF:TNFR complexes. We show that ectopic expression of Egr results in internalisation of Egr:Grnd complexes in vesicles, a step preceding and strictly required for Egr-induced apoptosis. We further demonstrate that Wgn binds Egr with much reduced affinity and is localised in intracellular vesicles that are distinct from those containing Egr:Grnd complexes. Altogether, our data provide insight into ligand-mediated activation of Grnd and suggest that distinct affinities of TNF ligands for their receptors promote different and non-redundant cellular functions.

Indexed as

Amino Acid SequenceAnimalsApoptosisCytoplasmic VesiclesDrosophila melanogasterDrosophila ProteinsEndocytosisImaginal DiscsMembrane ProteinsProtein BindingProtein DomainsProtein Interaction MappingReceptors, Tumor Necrosis FactorDrosophila Proteinsegr protein, Drosophilagrnd protein, DrosophilaMembrane ProteinsReceptors, Tumor Necrosis Factorwgn protein, Drosophila

Identifiers

PMID33824334
PMCPMC8024323
OpenAlexW3149404576

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.