Promyelocytic Leukemia Protein Interacts with the Apoptosis-associated Speck-like Protein to Limit Inflammasome Activation
| Autor: | Susan R. Quinn, Christine Becker, Dympna J. Connolly, Pier Paolo Pandolfi, Nollaig M. Bourke, Luke A. J. O'Neill, Sinéad C. Corr, Jennifer K. Dowling, Ashley Mansell |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
endocrine system
Inflammasomes animal diseases medicine.medical_treatment Immunology Inflammation macromolecular substances Promyelocytic Leukemia Protein Biology Biochemistry Promyelocytic leukemia protein AIM2 Cytosol Cell Line Tumor NLR Family Pyrin Domain-Containing 3 Protein medicine Humans Nuclear protein Molecular Biology Transcription factor Cell Nucleus Macrophages Tumor Suppressor Proteins Nuclear Proteins hemic and immune systems Inflammasome Cell Biology eye diseases Cell biology CARD Signaling Adaptor Proteins DNA-Binding Proteins Cytoskeletal Proteins HEK293 Cells Cytokine biology.protein Protein Multimerization medicine.symptom Carrier Proteins tissues Transcription Factors medicine.drug |
| Zdroj: | Journal of Biological Chemistry. 289:6429-6437 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m113.539692 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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