TY - JOUR
T1 - Death, TIR, and RHIM
T2 - Self-assembling domains involved in innate immunity and cell-death signaling
AU - Nanson, Jeffrey D.
AU - Kobe, Bostjan
AU - Ve, Thomas
N1 - Funding Information:
The work in the authors’ laboratories was supported by the National Health and Medical Research Council (NHMRC grants 1107804, 1071659, and 1003326). B.K. is an NHMRC Principal Research Fellow (1003325, 1110971), and T.V. is funded by an Australian Research Council Discovery Early Career Research Award (DE170100783).
Publisher Copyright:
©2018 Society for Leukocyte Biology
PY - 2019/2
Y1 - 2019/2
N2 - The innate immune system consists of pattern recognition receptors (PRRs) that detect pathogen- and 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.
AB - The innate immune system consists of pattern recognition receptors (PRRs) that detect pathogen- and 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.
KW - higher-order assembly signaling
KW - inflammasome
KW - necrosome
KW - NOD (nucleotide binding and oligomerization domain) and leucine rich repeat containing receptor (NLR)
KW - signaling by cooperative assembly formation (SCAF)
KW - Toll-like receptor
UR - http://www.scopus.com/inward/record.url?scp=85057751917&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85057751917&partnerID=8YFLogxK
U2 - 10.1002/JLB.MR0318-123R
DO - 10.1002/JLB.MR0318-123R
M3 - Review article
C2 - 30517972
AN - SCOPUS:85057751917
SN - 1938-3673
VL - 105
SP - 363
EP - 375
JO - Journal of Leukocyte Biology
JF - Journal of Leukocyte Biology
IS - 2
ER -