Structural Evolution of TIR-Domain Signalosomes
TIR (Toll/interleukin-1 receptor/resistance protein) domains are cytoplasmic domains widely found in animals and plants, where they are essential components of the innate immune system. A key feature of TIR-domain function in signaling is weak and transient self-association and association with othe...
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Frontiers Media S.A.
2021
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oai:doaj.org-article:ece1b08c56e44d039e4b4de42f74e8562021-11-17T05:39:22ZStructural Evolution of TIR-Domain Signalosomes1664-322410.3389/fimmu.2021.784484https://doaj.org/article/ece1b08c56e44d039e4b4de42f74e8562021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fimmu.2021.784484/fullhttps://doaj.org/toc/1664-3224TIR (Toll/interleukin-1 receptor/resistance protein) domains are cytoplasmic domains widely found in animals and plants, where they are essential components of the innate immune system. A key feature of TIR-domain function in signaling is weak and transient self-association and association with other TIR domains. An additional new role of TIR domains as catalytic enzymes has been established with the recent discovery of NAD+-nucleosidase activity by several TIR domains, mostly involved in cell-death pathways. Although self-association of TIR domains is necessary in both cases, the functional specificity of TIR domains is related in part to the nature of the TIR : TIR interactions in the respective signalosomes. Here, we review the well-studied TIR domain-containing proteins involved in eukaryotic immunity, focusing on the structures, interactions and their corresponding functional roles. Structurally, the signalosomes fall into two separate groups, the scaffold and enzyme TIR-domain assemblies, both of which feature open-ended complexes with two strands of TIR domains, but differ in the orientation of the two strands. We compare and contrast how TIR domains assemble and signal through distinct scaffolding and enzymatic roles, ultimately leading to distinct cellular innate-immunity and cell-death outcomes.Surekha NimmaWeixi GuNatsumi MarutaYan LiMengqi PanForhad Karim SaikotBryan Y. J. LimHelen Ying McGuinnessZannati Ferdous ZaotiSulin LiSneha DesaMohammad Kawsar ManikJeffrey D. NansonBostjan KobeFrontiers Media S.A.articleprotein structureprotein-protein interactionsaxon degenerationcell-death signalingsignaling by cooperative assembly formation (SCAF)innate immunityImmunologic diseases. AllergyRC581-607ENFrontiers in Immunology, Vol 12 (2021) |
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protein structure protein-protein interactions axon degeneration cell-death signaling signaling by cooperative assembly formation (SCAF) innate immunity Immunologic diseases. Allergy RC581-607 |
spellingShingle |
protein structure protein-protein interactions axon degeneration cell-death signaling signaling by cooperative assembly formation (SCAF) innate immunity Immunologic diseases. Allergy RC581-607 Surekha Nimma Weixi Gu Natsumi Maruta Yan Li Mengqi Pan Forhad Karim Saikot Bryan Y. J. Lim Helen Ying McGuinness Zannati Ferdous Zaoti Sulin Li Sneha Desa Mohammad Kawsar Manik Jeffrey D. Nanson Bostjan Kobe Structural Evolution of TIR-Domain Signalosomes |
description |
TIR (Toll/interleukin-1 receptor/resistance protein) domains are cytoplasmic domains widely found in animals and plants, where they are essential components of the innate immune system. A key feature of TIR-domain function in signaling is weak and transient self-association and association with other TIR domains. An additional new role of TIR domains as catalytic enzymes has been established with the recent discovery of NAD+-nucleosidase activity by several TIR domains, mostly involved in cell-death pathways. Although self-association of TIR domains is necessary in both cases, the functional specificity of TIR domains is related in part to the nature of the TIR : TIR interactions in the respective signalosomes. Here, we review the well-studied TIR domain-containing proteins involved in eukaryotic immunity, focusing on the structures, interactions and their corresponding functional roles. Structurally, the signalosomes fall into two separate groups, the scaffold and enzyme TIR-domain assemblies, both of which feature open-ended complexes with two strands of TIR domains, but differ in the orientation of the two strands. We compare and contrast how TIR domains assemble and signal through distinct scaffolding and enzymatic roles, ultimately leading to distinct cellular innate-immunity and cell-death outcomes. |
format |
article |
author |
Surekha Nimma Weixi Gu Natsumi Maruta Yan Li Mengqi Pan Forhad Karim Saikot Bryan Y. J. Lim Helen Ying McGuinness Zannati Ferdous Zaoti Sulin Li Sneha Desa Mohammad Kawsar Manik Jeffrey D. Nanson Bostjan Kobe |
author_facet |
Surekha Nimma Weixi Gu Natsumi Maruta Yan Li Mengqi Pan Forhad Karim Saikot Bryan Y. J. Lim Helen Ying McGuinness Zannati Ferdous Zaoti Sulin Li Sneha Desa Mohammad Kawsar Manik Jeffrey D. Nanson Bostjan Kobe |
author_sort |
Surekha Nimma |
title |
Structural Evolution of TIR-Domain Signalosomes |
title_short |
Structural Evolution of TIR-Domain Signalosomes |
title_full |
Structural Evolution of TIR-Domain Signalosomes |
title_fullStr |
Structural Evolution of TIR-Domain Signalosomes |
title_full_unstemmed |
Structural Evolution of TIR-Domain Signalosomes |
title_sort |
structural evolution of tir-domain signalosomes |
publisher |
Frontiers Media S.A. |
publishDate |
2021 |
url |
https://doaj.org/article/ece1b08c56e44d039e4b4de42f74e856 |
work_keys_str_mv |
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