FEBS Lett 2002,
PMID: 12459498
Kanamori, Mutsumi; Kai, Chikatoshi; Hayashizaki, Yoshihide; Suzuki, Harukazu
NF-kappaB activator 1 (Act1), also called CIKS, is a recently identified protein with NF-kappaB and AP-1 activation activities through its association with the IkappaB kinase complex. We identified and confirmed that Act1 interacts with tumor necrosis factor receptor-associated factor 6 (TRAF6); notably, Act1 binds to TRAF6 only among TRAF family proteins. The amino-terminal half of Act1 is required for its interaction with the TRAF domain. Act1-mediated NF-kappaB activation was inhibited by a dominant-negative mutant of TRAF6 in a dose-dependent manner, and IL-1-induced NF-kappaB activation was inhibited by a high level of Act1 expression. Our results suggest that Act1 is involved in IL-1/Toll-mediated signaling through TRAF6.
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Text Mining Data
NF-kappaB ⊣ TRAF6: "
Act1 mediated
NF-kappaB activation was
inhibited by a dominant negative mutant of
TRAF6 in a dose dependent manner, and IL-1 induced NF-kappaB activation was inhibited by a high level of Act1 expression
"
NF-kappaB ⊣ Act1: "
Act1 mediated NF-kappaB activation was inhibited by a dominant negative mutant of TRAF6 in a dose dependent manner, and IL-1 induced NF-kappaB activation was inhibited by a high level of Act1 expression
"
NF-kappaB ⊣ IL-1: "
Act1 mediated NF-kappaB activation was inhibited by a dominant negative mutant of TRAF6 in a dose dependent manner, and IL-1 induced NF-kappaB activation was inhibited by a high level of Act1 expression
"
Manually curated Databases
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IRef Biogrid Interaction:
TRAF6
—
TRAF3IP2
(direct interaction, two hybrid)
-
IRef Biogrid Interaction:
TRAF6
—
TRAF3IP2
(direct interaction, pull down)
-
IRef Biogrid Interaction:
TRAF6
—
TRAF3IP2
(physical association, affinity chromatography technology)
-
IRef Hprd Interaction:
TRAF6
—
TRAF3IP2
(in vitro)
-
IRef Hprd Interaction:
TRAF6
—
TRAF3IP2
(in vivo)
-
IRef Ophid Interaction:
TRAF6
—
TRAF3IP2
(aggregation, confirmational text mining)
In total, 1 gene pairs are associated to this article in curated databases