Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation
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2014Access:
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Dowling, J.K., Becker, C.E., Bourke, N.M., (...), Mansell, A., O'Neill, L.A.J., Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation, Journal of Biological Chemistry, 289, 10, 2014, 6429-6437Download Item:
J. Biol. Chem.-2014-Dowling-6429-37(1).pdf (PDF) 1.690Mb
Abstract:
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's Homepage:
http://people.tcd.ie/laoneillhttp://people.tcd.ie/corrsc
http://people.tcd.ie/nbourke
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Journal of Biological Chemistry289
10
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CancerSubject (TCD):
Immunology, Inflammation & InfectionDOI:
http://dx.doi.org/10.1074/jbc.M113.539692Licences: