ArticleCell death & disease2022
GSDMEa-mediated pyroptosis is bi-directionally regulated by caspase and required for effective bacterial clearance in teleost.
Article in Cell death & disease, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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.
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.
Who cites it
20 citing papers in PubMed, 57 citations in OpenAlex.
- Article
- Caspase-mediated interleukin-18 maturation promotes membrane-associated unconventional secretion and signal transduction in a teleost fish.Marine life science & technology · 2026Article
- Teleost GSDMEc regulates GSDMEa-mediated pyroptosis.Journal of advanced research · 2026Article
- Ninjurin-1 executes plasma membrane rupture and impairs anti-microbial immunity in an early jawed vertebrate.Cellular and molecular life sciences : CMLS · 2025Article
- Article
- Friend for the host foe for the guest: Evidence from probioticiMetaOmics · 2025Article
- Pufferfish gasdermin Ea is a significant player in the defense against bacterial pathogens.Marine life science & technology · 2024Article
- Characterization of the Apoptotic and Antimicrobial Activities of Two Initiator Caspases of Sea CucumberGenes · 2024Article
- Caspase-1 activates gasdermin A in non-mammals.eLife · 2024Article
- The molecular mechanism and evolutionary divergence of caspase 3/7-regulated gasdermin E activation.eLife · 2024Article
- Article
- An intracellular bacterial pathogen triggers RIG-I/MDA5-dependent necroptosis.Current research in microbial sciences · 2024Article
- Molecular mechanisms of gasdermin D pore-forming activity.Nature immunology · 2023Review
- Characterization of GSDME in amphioxus provides insights into the functional evolution of GSDM-mediated pyroptosis.PLoS biology · 2023Article
- An ancient defense mechanism: Conservation of gasdermin-mediated pyroptosis.PLoS biology · 2023Article
- Tongue sole creatine kinases function as DAMP and activate antimicrobial immunityFrontiers in immunology · 2023Article
- Emerging mechanisms and functions of inflammasome complexes in teleost fish.Frontiers in immunology · 2023Review
- A Non-Canonical Teleost NK-Lysin: Antimicrobial Activity via Multiple Mechanisms.International journal of molecular sciences · 2022Article
- Duck gasdermin E is a substrate of caspase-3/-7 and an executioner of pyroptosis.Frontiers in immunology · 2022Article
- New insights into the evolutionary dynamic and lineage divergence of gasdermin E in metazoa.Frontiers in cell and developmental biology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gasdermin (GSDM) is a family of pore-forming proteins that, after cleavage by caspase (CASP), induce a type of programmed necrotic cell death called pyroptosis. Gasdermin E (GSDME) is the only pyroptosis-inducing member of the GSDM family existing in teleost. To date, the regulation and function of teleost GSDME in response to bacterial infection remain elusive. In this study, we observed activation of GSDME, as well as multiple CASPs, in turbot Scophthalmus maximus during the infection of the bacterial pathogen Vibrio harveyi. Turbot has two GSDME orthologs named SmGSDMEa and SmGSDMEb. We found that SmGSDMEa was specifically cleaved by turbot CASP (SmCASP) 3/7 and SmCASP6, which produced two different N-terminal (NT) fragments. Only the NT fragment produced by SmCASP3/7 cleavage was able to induce pyroptosis. Ectopically expressed SmCASP3/7 activated SmGSDMEa, resulting in pyroptotic cell death. In contrast, SmCASP6 inactivated SmGSDMEa by destructive cleavage of the NT domain, thus nullifying the activation effect of SmCASP3/7. Unlike SmGSDMEa, SmGSDMEb was cleaved by SmCASP8 and unable to induce cell death. V. harveyi infection dramatically promoted the production and activation of SmGSDMEa, but not SmGSDMEb, and caused pyroptosis in turbot. Interference with SmCASP3/7 activity significantly enhanced the invasiveness and lethality of V. harveyi in a turbot infection model. Together, these results revealed a previously unrecognized bi-directional regulation mode of GSDME-mediated pyroptosis, and a functional difference between teleost GSDMEa and GSDMEb in the immune defense against bacterial infection.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.