Death, TIR, and RHIM: Self-assembling domains involved in innate immunity and cell-death signaling

Journal of Leukocyte Biology: An Official Publication of the Reticuloendothelial Society

article

Jeffrey D. Nanson¹  Bostjan Kobe¹  Thomas Ve¹ 

[1] School of Chemistry and Molecular Biosciences, Institute for Molecular Bioscience and Australian Infectious Diseases Research Centre, University of Queensland;Institute for Glycomics, Griffith University

关键词: higher-order assembly signaling;    inflammasome;    NOD (nucleotide binding and oligomerization domain) and leucine rich repeat containing receptor (NLR);    necrosome;    signaling by cooperative assembly formation (SCAF);    Toll-like receptor;   

DOI  :  10.1002/JLB.MR0318-123R

学科分类：生理学

来源: Federation of American Societies for Experimental Biology

【 摘 要 】

The innate immune system consists of pattern recognition receptors (PRRs) that detect pathogenand endogenous danger-associated molecular patterns (PAMPs and DAMPs), initiating signaling pathways that lead to the induction of cytokine expression, processing of pro-inflammatory cytokines, and induction of cell-death responses. An emerging concept in these pathways and associated processes is signaling by cooperative assembly formation (SCAF), which involves formation of higher order oligomeric complexes, and enables rapid and strongly amplified signaling responses to minute amounts of stimulus. Many of these signalosomes assemble through homotypic interactions of members of the death-fold (DF) superfamily, Toll/IL-1 receptor (TIR) domains, or the RIP homotypic interaction motifs (RHIM). We review the current understanding of the structure and function of these domains and their molecular interactions with a particular focus on higher order assemblies.

【 授权许可】

CC BY