Abstract

Inflammation is a crucial element of the host response to cellular insult. Pathogen-induced inflammation includes a molecular pathway which proceeds through activation of the protease caspase-1 to the release of the inflammatory cytokines interleukin-1 (IL-1) and IL-18. Importantly, pathogens may also induce forms of cell death that have inherently pro-inflammatory features. Here, we review recent evidence demonstrating that NLR (nucleotide-binding domain, leucine-rich repeat containing) family proteins serve as a common component of both caspase-1-activated apoptotic pathways and caspase-independent necrotic pathways. Parallels are drawn between NLR protein function and the activity of structurally similar proteins involved in cell death: the apoptotic mediator APAF1 (apoptotic-protease-activating factor 1) and the plant disease resistance NBS-LRR (nucleotide-binding site leucine-rich repeats) proteins.

Author affiliations

1. Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7295, USA.
2. Department of Microbiology and Immunology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7295, USA.
3. Curriculum in Genetics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7295, USA.
4. Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7295, USA.

Correspondence to: Jenny P.-Y. Ting^1,2,3 Email: jenny_ting@med.unc.edu

MORE ARTICLES LIKE THIS

These links to content published by NPG are automatically generated.