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dc.contributor.authorO'NEILL, LUKEen
dc.date.accessioned2016-01-06T15:26:32Z
dc.date.available2016-01-06T15:26:32Z
dc.date.issued2014en
dc.date.submitted2014en
dc.identifier.citationDowling 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, 6429-37en
dc.identifier.issn0021-9258en
dc.identifier.otherYen
dc.identifier.urihttp://hdl.handle.net/2262/75439
dc.descriptionPUBLISHEDen
dc.description.abstractThe 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.en
dc.format.extent6429-37en
dc.relation.ispartofseriesThe Journal of biological chemistryen
dc.relation.ispartofseries289en
dc.relation.ispartofseries10en
dc.rightsYen
dc.subjectCanceren
dc.titlePromyelocytic leukemia protein interacts with the apoptosis-associated speck-like protein to limit inflammasome activation.en
dc.typeJournal Articleen
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/laoneillen
dc.identifier.rssinternalid109629en
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M113.539692en
dc.rights.ecaccessrightsopenAccess


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