2017
DOI: 10.1016/j.dci.2017.01.014
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Diversity and evolution of TIR-domain-containing proteins in bivalves and Metazoa: New insights from comparative genomics

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Cited by 45 publications
(58 citation statements)
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References 108 publications
(98 reference statements)
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“…The TIR domain is found in a number of proteins linked to the detection of foreign ligands and to the ransduction of immune signals inside the cell. In detail, the expression of the cytosolic gene products MyD88, STING and ecTIR-DC families 6, 11 and 13 was particularly elevated in this tissue [89]. Moreover, a number of LITAF-like transcription factors, which may positively regulate the production of pro-inflammatory cytokines [90], were also selectively expressed in the gills.…”
Section: Resultsmentioning
confidence: 99%
“…The TIR domain is found in a number of proteins linked to the detection of foreign ligands and to the ransduction of immune signals inside the cell. In detail, the expression of the cytosolic gene products MyD88, STING and ecTIR-DC families 6, 11 and 13 was particularly elevated in this tissue [89]. Moreover, a number of LITAF-like transcription factors, which may positively regulate the production of pro-inflammatory cytokines [90], were also selectively expressed in the gills.…”
Section: Resultsmentioning
confidence: 99%
“…Some of these receptors are intracellular, e.g. the plant TNL and many invertebrate intracellular TIR domain‐containing proteins . In addition, some TIR‐containing proteins are used as adapters in the signaling pathway of the TIR receptors (e.g.…”
Section: Discussionmentioning
confidence: 99%
“…The IL‐1R‐like proteins in invertebrates, characterized by 2 Ig‐like domains, have scarce sequence homology with the vertebrate IL‐1R. As structurally conserved IL‐1 cytokines have not been unequivocally identified in invertebrates, the Ig/TIR domain combination of invertebrates has probably evolved independently, as it seems to have happened repeatedly in metazoan evolution . The putative absence of IL‐1 homologs in invertebrates suggests that Ig/TIR domain combination might have evolved in invertebrates for expanding their recognition and defensive capacity, exploiting the capacity of somatic recombination of Ig domains to generate a large number of molecules with distinct recognition specificity .…”
Section: Discussionmentioning
confidence: 99%
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“…Just as the dual function of MyD88 signaling in intestine, MyD88 signaling in IECs promotes expression of selective antimicrobial peptide, which associate enhanced host resistance and survival, but after infection with the H hepaticus, innate cell-derived MyD88 signaling promote inflammatory gene expression leading to colitis and extra-intestinal inflammation. In nature, the binding surfaces or interfaces of TIR domain are highly conserved (Gerdol et al, 2017). That is, different proteins containing TIR domain in TLR signaling world use the similar interfaces to interact with their partners.…”
mentioning
confidence: 99%