Evidence map›Paper›PMID 28656979›Full record

ArticleNature communications2017

MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism.

Xuan Li, Sarah Thome, Xiaodan Ma, Mamta Amrute-Nayak, Alison Finigan, Lauren Kitt, Leanne Masters, John R James, Yuguang Shi, Guoyu Meng and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

97 citing papers in PubMed, 1 synthesis or guideline pooled it.

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  11. Diverse Scaffolds Facilitate NLRP3 Clustering and Inflammasome Formation in Response to Perturbations in Cell Homeostasis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
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37 more citing papers are in PubMed but not listed here.

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.

Xuan LiDepartment of Medicine, University of Cambridge, The West Forvie Building, Robinson Way, Cambridge, CB2 0SZ, UK.
Sarah ThomeDepartment of Medicine, University of Cambridge, The West Forvie Building, Robinson Way, Cambridge, CB2 0SZ, UK.
Xiaodan MaState Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, Rui-Jin Hospital affiliated to Shanghai JiaoTong University School of Medicine, 197 Ruijin Er Road, Shanghai 200025, China.
Mamta Amrute-NayakDepartment of Molecular and Cell Physiology, Hannover Medical School, D-30625 Hannover, Germany.
Alison FiniganDepartment of Medicine, University of Cambridge, The West Forvie Building, Robinson Way, Cambridge, CB2 0SZ, UK.
Lauren KittDepartment of Medicine, University of Cambridge, The West Forvie Building, Robinson Way, Cambridge, CB2 0SZ, UK.
Leanne MastersDepartment of Medicine, University of Cambridge, The West Forvie Building, Robinson Way, Cambridge, CB2 0SZ, UK.
John R JamesMolecular Immunity Unit, Department of Medicine, University of Cambridge, MRC-LMB, Francis Crick Avenue, Cambridge, CB2 0QH, UK.ORCID 0000-0003-1452-7578
Yuguang ShiBarshop Institute for longevity and Aging Studies, University of Texas Health Science Center at San Antonio. Texas Research Park Campus MC 7755, 15355 Lamda Drive, San Antonio, Texas 78245, USA.
Guoyu MengState Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, Rui-Jin Hospital affiliated to Shanghai JiaoTong University School of Medicine, 197 Ruijin Er Road, Shanghai 200025, China.ORCID 0000-0001-7904-2382
Ziad MallatDepartment of Medicine, University of Cambridge, The West Forvie Building, Robinson Way, Cambridge, CB2 0SZ, UK.ORCID 0000-0003-0443-7878

Funding

British Heart Foundation FS/14/28/30713
6 · The paper itself

Abstract

Excessive activation of the NLR family pyrin domain containing 3 (NLRP3) inflammasome is involved in many chronic inflammatory diseases, including cardiovascular and Alzheimer's disease. Here we show that microtubule-affinity regulating kinase 4 (MARK4) binds to NLRP3 and drives it to the microtubule-organizing centre, enabling the formation of one large inflammasome speck complex within a single cell. MARK4 knockdown or knockout, or disruption of MARK4-NLRP3 interaction, impairs NLRP3 spatial arrangement and limits inflammasome activation. Our results demonstrate how an evolutionarily conserved protein involved in the regulation of microtubule dynamics orchestrates NLRP3 inflammasome activation by controlling its transport to optimal activation sites, and identify a targetable function for MARK4 in the control of innate immunity.

Indexed as

AnimalsHumansInflammasomesInterleukin-1betaMacrophagesMaleMiceMicrotubule-Organizing CenterMicrotubulesNLR Family, Pyrin Domain-Containing 3 ProteinPrimary Cell CultureProtein Serine-Threonine KinasesIL1B protein, mouseInflammasomesInterleukin-1betaMARK4 protein, mouseNLR Family, Pyrin Domain-Containing 3 ProteinNlrp3 protein, mouseProtein Serine-Threonine Kinases

Identifiers

PMID28656979
PMCPMC5493753

What OpenQuestion holds

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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.