Related Experiment Video
Updated: Feb 27, 2026

Detection of Inflammasome Activation and Pyroptotic Cell Death in Murine Bone Marrow-derived Macrophages
Published on: May 21, 2018
MARK4 regulates NLRP3 positioning and inflammasome activation through a microtubule-dependent mechanism
Xuan Li1, Sarah Thome1, Xiaodan Ma2
1Department of Medicine, University of Cambridge, The West Forvie Building, Robinson Way, Cambridge, CB2 0SZ, UK.
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.
More Related Videos
Related Concept Videos
Microtubule Associated Proteins (MAPs)
Mechanism of Filopodia Formation
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Regulation of Nuclear Protein Sorting
Mechanism of Lamellipodia Formation
NF-κB-dependent Signaling Pathway
NF-κB-dependent Signaling Mechanism
The...
Regulation of the Unfolded Protein Response

