loading...| Preferred Name | Recruitment of IKK complex | |
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Reviewed: Kawai, T, Akira, S, 2010-10-30 Edited: Garapati, P V, 2010-08-02 The molecular mechanisms by which caspase-8/10 attribute to NF-kB signaling is unclear. Caspase-8 might act as a scaffolding protein by bringing the IKK-complex in close proximity to its activator TAK1. The prodomain of Caspase-8 could interact with IKK2 in the IKK complex whereas the protease homology domain failed to do so. These results indicate that the interaction of the DEDs-containing prodomain of caspase-8 with the IKKs may be crucial for the NF-kB induction by caspase-8. Authored: Garapati, P V, 2010-08-02 |
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http://purl.obolibrary.org/obo/HINO_0007942 |
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Reviewed: Kawai, T, Akira, S, 2010-10-30 Edited: Garapati, P V, 2010-08-02 The molecular mechanisms by which caspase-8/10 attribute to NF-kB signaling is unclear. Caspase-8 might act as a scaffolding protein by bringing the IKK-complex in close proximity to its activator TAK1. The prodomain of Caspase-8 could interact with IKK2 in the IKK complex whereas the protease homology domain failed to do so. These results indicate that the interaction of the DEDs-containing prodomain of caspase-8 with the IKKs may be crucial for the NF-kB induction by caspase-8. Authored: Garapati, P V, 2010-08-02 |
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| definition source |
Pubmed12884866 Reactome, http://www.reactome.org Pubmed11002417 |
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Recruitment of IKK complex |
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HINO:0007942 |
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Recruitment of IKK complex |
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Reactome Database ID Release 43933539 ReactomeREACT_25134 |
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