loading...| Preferred Name | Multiple IRAK1 autophosphorylation steps | |
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| Definitions |
has a Stoichiometric coefficient of 16 Authored: de Bono, B, 2005-08-16 10:54:15 Reviewed: Gay, NJ, 2006-04-24 16:48:17 Phosphorylation of IRAK-1 is due to three sequential phosphorylation steps, which leads to full or hyper-phopshorylation of IRAK1. Under in vitro conditions these are all autophosphorylation events. First, Thr-209 is phosphorylated resulting in a conformational change of the kinase domain. Next, Thr-387 in the activation loop is phosphorylated, leading to full enzymatic activity. Several additional residues are phosphorylated in the proline-, serine-, and threonine-rich (ProST) region between the N-terminal death domain and kinase domain. Hyperphosphorylation of this region leads to dissociation of IRAK1 from the activated receptor complex. The kinase activity of IRAK1 is dispensable for IL1-induced NFkB and MAP kinase activation (Knop & Martin, 1999), unlike that of IRAK4 (Suzuki et al. 2002; Kozicak-Holbro et al. 2007), It has been suggested that IRAK1 primarily acts as an adaptor for TRAF6 (Conze et al. 2008). Reviewed: Napetschnig, Johanna, 2012-11-16 Edited: Shamovsky, V, 2012-11-06 Reviewed: Gillespie, ME, 2010-11-30 |
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http://purl.obolibrary.org/obo/HINO_0009127 |
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| comment |
has a Stoichiometric coefficient of 16 Authored: de Bono, B, 2005-08-16 10:54:15 Reviewed: Gay, NJ, 2006-04-24 16:48:17 Phosphorylation of IRAK-1 is due to three sequential phosphorylation steps, which leads to full or hyper-phopshorylation of IRAK1. Under in vitro conditions these are all autophosphorylation events. First, Thr-209 is phosphorylated resulting in a conformational change of the kinase domain. Next, Thr-387 in the activation loop is phosphorylated, leading to full enzymatic activity. Several additional residues are phosphorylated in the proline-, serine-, and threonine-rich (ProST) region between the N-terminal death domain and kinase domain. Hyperphosphorylation of this region leads to dissociation of IRAK1 from the activated receptor complex. The kinase activity of IRAK1 is dispensable for IL1-induced NFkB and MAP kinase activation (Knop & Martin, 1999), unlike that of IRAK4 (Suzuki et al. 2002; Kozicak-Holbro et al. 2007), It has been suggested that IRAK1 primarily acts as an adaptor for TRAF6 (Conze et al. 2008). Reviewed: Napetschnig, Johanna, 2012-11-16 Edited: Shamovsky, V, 2012-11-06 Reviewed: Gillespie, ME, 2010-11-30 |
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| definition source |
Pubmed18347055 Reactome, http://www.reactome.org Pubmed14625308 Pubmed17337443 Pubmed11923871 Pubmed10217414 |
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| label |
Multiple IRAK1 autophosphorylation steps |
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| prefixIRI |
HINO:0009127 |
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| prefLabel |
Multiple IRAK1 autophosphorylation steps |
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| seeAlso |
Reactome Database ID Release 43166286 ReactomeREACT_6862 |
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