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- Title
NF-kappaB activation through IKK-i-dependent I-TRAF/TANK phosphorylation.
- Authors
Nomura, F; Kawai, T; Nakanishi, K; Akira, S
- Abstract
NF-kappaB is an ubiquitously expressed transcription factor that plays an important role in the immune, anti-apoptotic and inflammatory responses. NF-kappaB is normally sequestered in the cytoplasm by interacting with inhibitory IkappaB molecules. Upon stimulation, IkappaB is phosphorylated and subsequently degraded by the proteasome, allowing NF-kappaB to translocate into the nucleus where they regulate target gene expression. Two kinases, IKK-alpha and IKK-beta, which are responsible for IkappaB phosphorylation were recently identified. We have recently identified a cytokine inducible IKK-i, a kinase related to IKK-alpha and -beta. IKK-i significantly induced NF-kappaB activation upon over-expression, as did IKK-alpha and IKK-beta. Unlike IKK-alpha and IKK-beta, IKK-i phosphorylated Ser36 but not Ser32 in vitro, suggesting that IKK-i activates NF-kappaB by distinct mechanisms from the conventional IKKs.
- Publication
Genes to cells : devoted to molecular & cellular mechanisms, 2000, Vol 5, Issue 3, p191
- ISSN
1356-9597
- Publication type
Journal Article
- DOI
10.1046/j.1365-2443.2000.00315.x