ArticleCell death & disease2016
The Yersinia Type III secretion effector YopM Is an E3 ubiquitin ligase that induced necrotic cell death by targeting NLRP3.
Article in Cell death & disease, 2016. 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, 43 citations in OpenAlex.
- Loss-of-function CARD8 mutation causes NLRP3 inflammasome activation and Crohn's disease.The Journal of clinical investigation · 2018Trial
- Comprehensive in silico analysis of eggNOG-annotated orthologous genes infers functional dynamics and energy metabolism in the microbiome of Abutilon fruticosum.BMC plant biology · 2026Article
- Targeting Undruggable Protein Interactions with DNA Aptamers: Inhibition of the Interaction BetweenInternational journal of molecular sciences · 2026Article
- TheBiochemistry · 2024Article
- Legionella effectors SidC/SdcA ubiquitinate multiple small GTPases and SNARE proteins to promote phagosomal maturation.Cellular and molecular life sciences : CMLS · 2024Article
- New insights into the putative role of leucine-rich repeat proteins ofFrontiers in cellular and infection microbiology · 2024Review
- Ubiquitin-targeted bacterial effectors: rule breakers of the ubiquitin system.The EMBO journal · 2023Review
- EspE3 plays a role in the pathogenicity of avian pathogenic Escherichia coli.Veterinary research · 2023Article
- The NEL Family of Bacterial E3 Ubiquitin Ligases.International journal of molecular sciences · 2022Review
- Role of the Yersinia pseudotuberculosis Virulence Plasmid in Pathogen-Phagocyte Interactions in Mesenteric Lymph Nodes.EcoSal Plus · 2021Review
- Bacterial nucleomodulins: A coevolutionary adaptation to the eukaryotic command center.PLoS pathogens · 2021Review
- The pyrin inflammasome and the Yersinia effector interaction.Immunological reviews · 2020Review
- Review
- Redundant and Cooperative Roles for Yersinia pestis Yop Effectors in the Inhibition of Human Neutrophil Exocytic Responses Revealed by Gain-of-Function Approach.Infection and immunity · 2020Article
- TheFrontiers in cellular and infection microbiology · 2020Article
- Yersinia pestis and plague: an updated view on evolution, virulence determinants, immune subversion, vaccination, and diagnostics.Genes and immunity · 2019Review
- Ubiquitination-Mediated Inflammasome Activation during Bacterial Infection.International journal of molecular sciences · 2019Review
- Bacterial LPX motif-harboring virulence factors constitute a species-spanning family of cell-penetrating effectors.Cellular and molecular life sciences : CMLS · 2018Article
- Ubiquitin-Modifying Enzymes and Regulation of the Inflammasome.Journal of molecular biology · 2017Review
- Immunomodulatory Yersinia outer proteins (Yops)-useful tools for bacteria and humans alike.Virulence · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
17 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Yersinia pestis uses type III effector proteins to target eukaryotic signaling systems. The Yersinia outer protein (Yop) M effector from the Y. pestis strain is a critical virulence determinant; however, its role in Y. pestis pathogenesis is just beginning to emerge. Here we first identify YopM as the structural mimic of the bacterial IpaH E3 ligase family in vitro, and establish that the conserved CLD motif in its N-terminal is responsible for the E3 ligase function. Furthermore, we show that NLRP3 is a novel target of the YopM protein. Specially, YopM associates with NLRP3, and its CLD ligase motif mediates the activating K63-linked ubiquitylation of NLRP3; as a result, YopM modulates NLRP3-mediated cell necrosis. Mutation of YopM E3 ligase motif dramatically reduces the ability of Y. pestis to induce HMGB1 release and cell necrosis, which ultimately contributes to bacterial virulence. In conclusion, this study has identified a previously unrecognized role for YopM E3 ligase activity in the regulation of host cell necrosis and plague pathogenesis.
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.