loading...| Preferred Name | Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon | |
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Reviewed: Fitzgerald, Katherine A, 2012-11-13 Cell stimulation with viral ds RNA leads to the activation of two IKK-related serine/threonine kinases, TBK1 and IKK-i which directly phosphorylate IRF3 and IRF7 promoting their dimerization and translocation into the nucleus. Although both kinases show structural and functional similarities, it seems that TBK1 and IKK-i differ in their regulation of downstream signaling events of TLR3.<p>IRF3 activation and IFN-b production by poly(I:C) are decreased in TBK1-deficient mouse fibroblasts, whereas normal activation was observed in the IKK-i-deficient fibroblasts. However, in double-deficient mouse fibroblasts, the activation of IRF3 is completely abolished, suggesting a partially redundant functions of TBK1 and IKK-i [Hemmi et al 2004].<p>TLR3 recruits and activates PI3 kinase (PI3K), which activates the downstream kinase, Akt, leading to full phosphorylation and activation of IRF-3 [Sarkar SN et al 2004]. When PI3K is not recruited to TLR3 or its activity is blocked, IRF-3 is only partially phosphorylated and fails to bind the promoter of the target gene. Reviewed: Gillespie, ME, 2010-11-30 Authored: Shamovsky, V, 2010-06-01 Edited: Shamovsky, V, 2010-11-16 |
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http://purl.obolibrary.org/obo/HINO_0022352 |
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Reviewed: Fitzgerald, Katherine A, 2012-11-13 Cell stimulation with viral ds RNA leads to the activation of two IKK-related serine/threonine kinases, TBK1 and IKK-i which directly phosphorylate IRF3 and IRF7 promoting their dimerization and translocation into the nucleus. Although both kinases show structural and functional similarities, it seems that TBK1 and IKK-i differ in their regulation of downstream signaling events of TLR3. IRF3 activation and IFN-b production by poly(I:C) are decreased in TBK1-deficient mouse fibroblasts, whereas normal activation was observed in the IKK-i-deficient fibroblasts. However, in double-deficient mouse fibroblasts, the activation of IRF3 is completely abolished, suggesting a partially redundant functions of TBK1 and IKK-i [Hemmi et al 2004]. TLR3 recruits and activates PI3 kinase (PI3K), which activates the downstream kinase, Akt, leading to full phosphorylation and activation of IRF-3 [Sarkar SN et al 2004]. When PI3K is not recruited to TLR3 or its activity is blocked, IRF-3 is only partially phosphorylated and fails to bind the promoter of the target gene. Reviewed: Gillespie, ME, 2010-11-30 Authored: Shamovsky, V, 2010-06-01 Edited: Shamovsky, V, 2010-11-16 |
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| definition source |
Pubmed15210742 Reactome, http://www.reactome.org Pubmed17332413 Pubmed15502848 Pubmed14679297 |
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Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon |
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HINO:0022352 |
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| prefLabel |
Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon |
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| seeAlso |
Reactome Database ID Release 43936964 GENE ONTOLOGYGO:0035666 ReactomeREACT_25148 |
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http://purl.obolibrary.org/obo/HINO_0009341 http://purl.obolibrary.org/obo/HINO_0009328 http://purl.obolibrary.org/obo/HINO_0009335 http://purl.obolibrary.org/obo/HINO_0009339 http://purl.obolibrary.org/obo/HINO_0009337 |