Evidence map›Paper›PMID 26492367›Full record

ArticleCell death & disease2015

Implication of different domains of the Leishmania major metacaspase in cell death and autophagy.

M Casanova, I J Gonzalez, C Sprissler, H Zalila, M Dacher, L Basmaciyan, G F Späth, N Azas, N Fasel

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

21 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. An inclusive assessment of apoptosis mechanisms inCurrent research in parasitology & vector-borne diseases · 2025
    Review
  4. Article
  5. Rational repurposing, synthesis,Journal of enzyme inhibition and medicinal chemistry · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Cell death in Leishmania.Parasite (Paris, France) · 2019
    Review
  15. Article
  16. Review
  17. Different apoptosis pathways inCell death discovery · 2018
    Article
  18. Article
  19. Article
  20. Article
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

9 authors at 4 institutions in 2 countries.

M CasanovaInfections Parasitaires, Transmission et Thérapeutique, UMR-MD3, Aix-Marseille University, Marseille, France.
I J GonzalezDepartment of Biochemistry, University of Lausanne, 155 Chemin des Boveresses, 1066 Epalinges, Switzerland.
C SprisslerDepartment of Biochemistry, University of Lausanne, 155 Chemin des Boveresses, 1066 Epalinges, Switzerland.
H ZalilaDepartment of Biochemistry, University of Lausanne, 155 Chemin des Boveresses, 1066 Epalinges, Switzerland.
M DacherInstitut Pasteur and Centre National de la Recherche Scientifique URA 2581, Unité de Parasitologie Moléculaire et Signalisation, Paris, France.
L BasmaciyanInfections Parasitaires, Transmission et Thérapeutique, UMR-MD3, Aix-Marseille University, Marseille, France.
G F SpäthInstitut Pasteur and Centre National de la Recherche Scientifique URA 2581, Unité de Parasitologie Moléculaire et Signalisation, Paris, France.
N AzasInfections Parasitaires, Transmission et Thérapeutique, UMR-MD3, Aix-Marseille University, Marseille, France.
N FaselDepartment of Biochemistry, University of Lausanne, 155 Chemin des Boveresses, 1066 Epalinges, Switzerland.
University of Lausanne · CHGénétique et Immunologie des Maladies Parasitaires · FRCentre National de la Recherche Scientifique · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metacaspases (MCAs) are cysteine peptidases expressed in plants, fungi and protozoa, with a caspase-like histidine-cysteine catalytic dyad, but differing from caspases, for example, in their substrate specificity. The role of MCAs is subject to debate: roles in cell cycle control, in cell death or even in cell survival have been suggested. In this study, using a Leishmania major MCA-deficient strain, we showed that L. major MCA (LmjMCA) not only had a role similar to caspases in cell death but also in autophagy and this through different domains. Upon cell death induction by miltefosine or H2O2, LmjMCA is processed, releasing the catalytic domain, which activated substrates via its catalytic dyad His/Cys and a proline-rich C-terminal domain. The C-terminal domain interacted with proteins, notably proteins involved in stress regulation, such as the MAP kinase LmaMPK7 or programmed cell death like the calpain-like cysteine peptidase. We also showed a new role of LmjMCA in autophagy, acting on or upstream of ATG8, involving Lmjmca gene overexpression and interaction of the C-terminal domain of LmjMCA with itself and other proteins. These results allowed us to propose two models, showing the role of LmjMCA in the cell death and also in the autophagy pathway, implicating different protein domains.

Indexed as

AutophagyCaspasesCell DeathGene Expression Regulation, EnzymologicLeishmania majorModels, BiologicalProtein Structure, TertiaryProtozoan ProteinsStress, PhysiologicalCaspasesProtozoan Proteins

Identifiers

PMID26492367
PMCPMC4632311
OpenAlexW2412330801

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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.