| First Author | Dowling JK | Year | 2014 |
| Journal | J Biol Chem | Volume | 289 |
| Issue | 10 | Pages | 6429-37 |
| PubMed ID | 24407287 | Mgi Jnum | J:219619 |
| Mgi Id | MGI:5621259 | Doi | 10.1074/jbc.M113.539692 |
| Citation | Dowling JK, et al. (2014) Promyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation. J Biol Chem 289(10):6429-37 |
| abstractText | 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-1beta 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. |
