Evidence map›Paper›PMID 36384135›Full record

ArticleImmunity2022

IKKβ primes inflammasome formation by recruiting NLRP3 to the trans-Golgi network.

Niklas A Schmacke, Fionan O'Duill, Moritz M Gaidt, Inga Szymanska, Julia M Kamper, Jonathan L Schmid-Burgk, Sophia C Mädler, Timur Mackens-Kiani, Tatsuya Kozaki, Dhruv Chauhan and 10 more

Open access · greenAbstract read
In one paragraph

Article in Immunity, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed, 1 pooled it
9.3field-weighted citation impact, top 1% 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

82 citing papers in PubMed, 1 synthesis or guideline pooled it, 119 citations in OpenAlex.

  1. Pooled it
  2. Review
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  4. Review
  5. Article
  6. Pyroptotic cell-derived factors promote osteoclast differentiation.bioRxiv : the preprint server for biology · 2026
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  8. Innate immunity: current understandings and future perspectives.Signal transduction and targeted therapy · 2026
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Mechanism of NLRP3 Inflammasome Activation and Its Roles in Chronic Rhinosinusitis.World journal of otorhinolaryngology - head and neck surgery · 2026
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. An overview of human inflammasomes: Activation and regulation.Journal of immunology (Baltimore, Md. : 1950) · 2026
    Review
  20. Article

22 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

20 authors at 3 institutions in 3 countries.

Niklas A SchmackeGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Fionan O'DuillGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Moritz M GaidtGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Inga SzymanskaGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Julia M KamperGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Jonathan L Schmid-BurgkGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Sophia C MädlerDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Timur Mackens-KianiGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Tatsuya KozakiSingapore Immunology Network (SIgN), Agency for Science, Technology & Research (A∗STAR), 8A Biomedical Grove, Immunos Building #3-4, Biopolis, Singapore 138648, Singapore.
Dhruv ChauhanGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Dennis NaglGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Che A StaffordGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Hartmann HarzFaculty of Biology, Human Biology and BioImaging, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
Adrian L FröhlichGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Francesca PinciGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Florent GinhouxSingapore Immunology Network (SIgN), Agency for Science, Technology & Research (A∗STAR), 8A Biomedical Grove, Immunos Building #3-4, Biopolis, Singapore 138648, Singapore; Shanghai Institute of Immunology, Shanghai JiaoTong University School of Medicine, 280 South Chongqing Road, Shanghai 200025, China; Translational Immunology Institute, SingHealth Duke-NUS Academic Medical Centre, Singapore 169856, Singapore.
Roland BeckmannGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
Matthias MannDepartment of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
Heinrich LeonhardtFaculty of Biology, Human Biology and BioImaging, Ludwig-Maximilians-Universität München, Planegg-Martinsried, Germany.
Veit HornungGene Center and Department of Biochemistry, Ludwig-Maximilians-Universität München, 81377 Munich, Germany. Electronic address: hornung@genzentrum.lmu.de.
Ludwig-Maximilians-Universität München · DEAgency for Science, Technology and Research · SGMax Planck Institute of Biochemistry · DE

Funding

European Research Council 101018672
6 · The paper itself

Abstract

The NLRP3 inflammasome plays a central role in antimicrobial defense as well as in the context of sterile inflammatory conditions. NLRP3 activity is governed by two independent signals: the first signal primes NLRP3, rendering it responsive to the second signal, which then triggers inflammasome formation. Our understanding of how NLRP3 priming contributes to inflammasome activation remains limited. Here, we show that IKKβ, a kinase activated during priming, induces recruitment of NLRP3 to phosphatidylinositol-4-phosphate (PI4P), a phospholipid enriched on the trans-Golgi network. NEK7, a mitotic spindle kinase that had previously been thought to be indispensable for NLRP3 activation, was redundant for inflammasome formation when IKKβ recruited NLRP3 to PI4P. Studying iPSC-derived human macrophages revealed that the IKKβ-mediated NEK7-independent pathway constitutes the predominant NLRP3 priming mechanism in human myeloid cells. Our results suggest that PI4P binding represents a primed state into which NLRP3 is brought by IKKβ activity.

Indexed as

InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinAnimalsHumansI-kappa B KinaseMiceMice, Inbred C57BLNIMA-Related KinasesProtein Serine-Threonine Kinasestrans-Golgi NetworkI-kappa B KinaseInflammasomesNIMA-Related KinasesNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mouseProtein Serine-Threonine Kinasesinflammasomeinnate immunityiPSCsmacrophagesmonocytesNEK7NLRP3pattern recognition

Identifiers

PMID36384135
PMCPMC7614333
OpenAlexW4309247510

What OpenQuestion holds

Textmetadata
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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.