Evidence map›Paper›PMID 37945612›Full record

ArticleNature communications2023

Cryo-electron tomography of NLRP3-activated ASC complexes reveals organelle co-localization.

Yangci Liu, Haoming Zhai, Helen Alemayehu, Jérôme Boulanger, Lee J Hopkins, Alicia C Borgeaud, Christina Heroven, Jonathan D Howe, Kendra E Leigh, Clare E Bryant and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

35 citing papers in PubMed, 33 citations in OpenAlex.

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  9. Plant NLRs are getting into higher-order architectures.The Plant journal : for cell and molecular biology · 2026
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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 4 countries.

Yangci LiuMolecular Immunity Unit, Department of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Haoming ZhaiMolecular Immunity Unit, Department of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Helen AlemayehuMolecular Immunity Unit, Department of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Jérôme BoulangerMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Lee J HopkinsDepartment of Medicine, University of Cambridge, Box 157, Level 5, Addenbrooke's Hospital, Cambridge, CB2 0QQ, UK.
Alicia C BorgeaudMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Christina HerovenMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Jonathan D HoweMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.ORCID http://orcid.org/0000-0001-7941-2486
Kendra E LeighMolecular Immunity Unit, Department of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.ORCID http://orcid.org/0000-0002-6467-3330
Clare E BryantDepartment of Medicine, University of Cambridge, Box 157, Level 5, Addenbrooke's Hospital, Cambridge, CB2 0QQ, UK. ceb27@cam.ac.uk.ORCID http://orcid.org/0000-0002-2924-0038
Yorgo ModisMolecular Immunity Unit, Department of Medicine, University of Cambridge, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK. ymodis@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0002-6084-0429
MRC Laboratory of Molecular Biology · GBUniversity of Cambridge · GBUniversity of Bern · CH

Funding

Wellcome Trust 101908/Z/13/ZWellcome Trust 217191
6 · The paper itself

Abstract

NLRP3 induces caspase-1-dependent pyroptotic cell death to drive inflammation. Aberrant activity of NLRP3 occurs in many human diseases. NLRP3 activation induces ASC polymerization into a single, micron-scale perinuclear punctum. Higher resolution imaging of this signaling platform is needed to understand how it induces pyroptosis. Here, we apply correlative cryo-light microscopy and cryo-electron tomography to visualize ASC/caspase-1 in NLRP3-activated cells. The puncta are composed of branched ASC filaments, with a tubular core formed by the pyrin domain. Ribosomes and Golgi-like or endosomal vesicles permeate the filament network, consistent with roles for these organelles in NLRP3 activation. Mitochondria are not associated with ASC but have outer-membrane discontinuities the same size as gasdermin D pores, consistent with our data showing gasdermin D associates with mitochondria and contributes to mitochondrial depolarization.

Indexed as

InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinCaspase 1CaspasesElectron Microscope TomographyGasderminsHumansOrganellesPyroptosisCaspase 1CaspasesGasderminsInflammasomesNLR Family, Pyrin Domain-Containing 3 Protein

Identifiers

PMID37945612
PMCPMC10636019
OpenAlexW4388523984

What OpenQuestion holds

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Registered trials

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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.