AI Article Synopsis
- The NLRP3 inflammasome's rapid formation and activation are initiated by the combined stimulation of LPS and nigericin, with IKKβ playing a crucial role.
- IKKβ's activation occurs independently of new protein production but is essential for positioning NLRP3 near TGN38 in the trans-Golgi network.
- Enhanced Golgi dispersion occurs with LPS co-stimulation, and inhibiting IKKβ prior to nigericin stimulation prevents the activation of the NLRP3 inflammasome.
Article Abstract
The rapid formation and activation of the NLRP3 inflammasome is induced by co-stimulation with LPS and nigericin. It requires the LPS-stimulated activation of IKKβ, which exerts its effects independently of de novo gene transcription, protein translation and other protein kinases activated by IKKβ. IKKβ is not required for the nigericin-induced dispersion of the trans-Golgi network (TGN), but to bring NLRP3 in proximity with TGN38. The nigericin-induced dispersion of the Golgi is enhanced by co-stimulation with LPS, and this enhancement is IKKβ-dependent. Prolonged stimulation with LPS to increase the expression of NLRP3, followed by stimulation with nigericin, produced larger TGN38-positive puncta, and the ensuing activation of the NLRP3 inflammasome was also suppressed by IKKβ inhibitors added prior to stimulation with nigericin. IKKβ therefore has a key role in recruiting NLRP3 to the dispersed TGN, leading to the formation and activation of the NLRP3 inflammasome.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8490994 | PMC |
| http://dx.doi.org/10.15252/embr.202050743 | DOI Listing |
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