The NLRP1 inflammasome: new mechanistic insights and unresolved mysteries
| Autor: | Patrick S. Mitchell, Russell E. Vance, Andrew Sandstrom |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Inflammasomes
Immunology Innate immunology NLR Proteins Computational biology Biology Article Genetics medicine Innate 2.1 Biological and endogenous factors Humans Immunology and Allergy Aetiology Cancer Adaptor Proteins Signal Transducing Innate immune system Effector NLRP1 Signal Transducing Immunity Adaptor Proteins Signal transducing adaptor protein Inflammasome Immunity Innate Neoplasm Proteins CARD Signaling Adaptor Proteins Mechanism (philosophy) Direct binding Apoptosis Regulatory Proteins medicine.drug |
| Zdroj: | Curr Opin Immunol |
| ISSN: | 0952-7915 |
| Popis: | Nucleotide-binding domain, leucine-rich repeat (NLR) proteins constitute a diverse class of innate immune sensors that detect pathogens or stress-associated stimuli in plants and animals. Some NLRs are activated upon direct binding to pathogen-derived ligands. In contrast, we focus here on a vertebrate NLR called NLRP1 that responds to the enzymatic activities of pathogen effectors. We discuss a newly proposed ‘functional degradation’ mechanism that explains activation and assembly of NLRP1 into an oligomeric complex called an inflammasome. We also discuss how NLRP1 is activated by non-pathogen-associated triggers such as the anti- cancer drug Val-boroPro, or by human disease-associated mutations. Finally, we discuss how research on NLRP1 has led to additional biological insights, including the unexpected discovery of a new CARD8 inflammasome. |
| Databáze: | OpenAIRE |
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