Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation.
Item Type:Journal Article
Citation:Dowling JK, Becker CE, Bourke NM, Corr SC, Connolly DJ, Quinn SR, Pandolfi PP, Mansell A, O'Neill LA, Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation., The Journal of biological chemistry, 289, 10, 2014, 6429-37
J. Biol. Chem.-2014-Dowling-6429-37.pdf (PDF) 1.690Mb
The apoptosis-associated speck-like protein containing a caspase-activating recruitment domain (ASC) is an essential component of several inflammasomes, multiprotein complexes that regulate caspase-1 activation and inflammation. We report here an interaction between promyelocytic leukemia protein (PML) and ASC. We observed enhanced formation of ASC dimers in PML-deficient macrophages. These macrophages also display enhanced levels of ASC in the cytosol. Furthermore, IL-1β production was markedly enhanced in these macrophages in response to both NLRP3 and AIM2 inflammasome activation and following bone marrow-derived macrophage infection with herpes simplex virus-1 (HSV-1) and Salmonella typhimurium. Collectively, our data indicate that PML limits ASC function, retaining ASC in the nucleus.
Author: O'NEILL, LUKE
Type of material:Journal Article
Series/Report no:The Journal of biological chemistry
Availability:Full text available