Skip to Main content Skip to Navigation
Journal articles

Caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop.

Abstract : The inflammasome is an innate immune signaling platform leading to caspase-1 activation, maturation of pro-inflammatory cytokines and cell death. Recognition of DNA within the host cytosol induces the formation of a large complex composed of the AIM2 receptor, the ASC adaptor and the caspase-1 effector. Francisella tularensis, the agent of tularemia, replicates within the host cytosol. The macrophage cytosolic surveillance system detects Francisella through the AIM2 inflammasome. Upon Francisella novicida infection, we observed a faster kinetics of AIM2 speck formation in ASC(KO) and Casp1(KO) as compared to WT macrophages. This observation was validated by a biochemical approach thus demonstrating for the first time the existence of a negative feedback loop controlled by ASC/caspase-1 that regulates AIM2 complex formation/stability. This regulatory mechanism acted before pyroptosis and required caspase-1 catalytic activity. Our data suggest that sublytic caspase-1 activity could delay the formation of stable AIM2 speck, an inflammasome complex associated with cell death.
Complete list of metadatas

https://hal.archives-ouvertes.fr/hal-00965029
Contributor : Laurence Naiglin <>
Submitted on : Monday, March 24, 2014 - 3:06:39 PM
Last modification on : Wednesday, April 22, 2020 - 9:42:04 AM

Links full text

Identifiers

Citation

C. Juruj, V. Lelogeais, R. Pierini, M. Perret, B. F. Py, et al.. Caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop.. Frontiers in Cellular and Infection Microbiology, Frontiers Media, 2013, 3, pp.14. ⟨10.3389/fcimb.2013.00014⟩. ⟨hal-00965029⟩

Share

Metrics

Record views

171