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Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation
O'NEILL, LUKE; QUINN, SUSAN; BOURKE, NOLLAIG; CORR, SINEAD
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-1? 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.
Keyword(s): Cancer; Immunology, Inflammation & Infection
Publication Date:
2014
Type: Journal article
Peer-Reviewed: Yes
Institution: Trinity College Dublin
Citation(s): 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, 6429-6437
First Indexed: 2016-01-07 05:10:11 Last Updated: 2020-10-30 07:49:37