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

Juruj, C. and Lelogeais, V. and Pierini, R. and Perret, M. and Py, B. F. and Jamilloux, Y. and Broz, P. and Ader, F. and Faure, M. and Henry, T.. (2013) Caspase-1 activity affects AIM2 speck formation/stability through a negative feedback loop. Frontiers in Cellular and Infection Microbiology, 3. p. 14.

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Official URL: http://edoc.unibas.ch/49022/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Infection Biology (Broz)
UniBasel Contributors:Broz, Petr
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Frontiers Media
e-ISSN:2235-2988
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:03 Oct 2017 09:58
Deposited On:03 Oct 2017 09:58

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