Fig. 3
From: An update on the regulatory mechanisms of NLRP3 inflammasome activation
Spatiotemporal regulation of the NLRP3 inflammasome complex. NLRP3, which is present in the endoplasmic reticulum (ER), comes in close proximity to apoptosis-associated speck-like protein containing a CARD (ASC) in mitochondria upon induction by various stimuli. It is known that NLRP3 and ASC are assembled in mitochondria-associated ER membranes (MAMs). NLRP3 binds to microtubule affinity regulating kinase 4 (MARK4) and is translocated to microtubule-organizing center (MTOC). When NLRP3 reaches the MTOC, NIMA related kinase 7 (NEK7) binds with NLRP3, and the inflammasome is assembled. In addition, NLRP3 is recruited to the dispersed trans-Golgi network (dTGN) through phosphatidylinositol-4-phosphate (PIP4) by diverse stimuli. In addition, translocation of the SREBP cleavage-activating protein (SCAP)-sterol regulatory element-binding protein 2 (SREBP2) complex from the ER to the Golgi is important for the activation of NLRP3. Diacylglycerol (DAG) in the Golgi recruits protein kinase D (PKD), which is involved in the assembly and activation of NLRP3
