IndraLab
Statements
IKK_complex binds TRAF2, TRAF6, and CYLD. 1 / 1
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"The initial clue to the signaling function of CYLD came from an RNAi-based functional screening study, which identified CYLD as a DUB that negatively regulates NF- κ B activation. xref At the same time, yeast two-hybrid screening studies identified CYLD as a protein that binds to NF- κ B essential modulator (NEMO), a regulatory subunit of I κ B kinase (IKK). xref , xref CoIP assays also revealed the association of CYLD with two IKK regulatory proteins, TRAF2 and TRAF6, and subsequent studies identified additional molecular targets of CYLD ( xref )."
reach
"The biochemical analysis using phosphomimetic mutants demonstrated that this PTM negatively affects the deubiquitinating activity of CYLD on TRAF2, most likely through interfering with the catalytic activity of CYLD, since the binding of TRAF2 to a CYLD mutant mimicking phosphorylation on Ser 418 is not affected."
reach
"Here we described that the adenoviral vector expressing CYLD (Ad/hTERT-CYLD) augmented the cytotoxicity of TRAIL in HCC cells by negatively regulating NF-kappaB activity since CYLD could reverse the ubiquitination of TNF receptor associated factor 2 (TRAF2) and interact with the IkappaB kinasegamma (IKKgamma)."
"We conclude that PrP traps CYLD, preventing it from binding and deubiquitinating RIP1 and TRAF2."
reach
"Similarly, de-ubiquitinating enzyme cylindromatosis (CYLD) inhibits NF-kappaB signaling via de-ubiquitination and inactivation of TNFR associated factor 2 (TRAF2) and TRAF6 [XREF_BIBR, XREF_BIBR]; de-ubiquitinating protease A20 inhibits NF-kappaB activation induced by Toll like receptor 4 (TLR4) via removing K63 linked polyubiquitin chains of TRAF6 [XREF_BIBR]."
reach
"The regulation of TRAF2 signaling by CYLD was identified by screening an RNAi library targeting DUBs for ones that attenuate NFkappaB activation [XREF_BIBR] and through a two-hybrid screen for proteins that interact with the regulatory subunit of the IkappaB kinase complex that could also bind to TRAF2 [XREF_BIBR]."
IKK_complex binds TRAF2, TRAF6, and CYLD. 1 / 1
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1
sparser
"The initial clue to the signaling function of CYLD came from an RNAi-based functional screening study, which identified CYLD as a DUB that negatively regulates NF- κ B activation. xref At the same time, yeast two-hybrid screening studies identified CYLD as a protein that binds to NF- κ B essential modulator (NEMO), a regulatory subunit of I κ B kinase (IKK). xref , xref CoIP assays also revealed the association of CYLD with two IKK regulatory proteins, TRAF2 and TRAF6, and subsequent studies identified additional molecular targets of CYLD ( xref )."
reach
"The biochemical analysis using phosphomimetic mutants demonstrated that this PTM negatively affects the deubiquitinating activity of CYLD on TRAF2, most likely through interfering with the catalytic activity of CYLD, since the binding of TRAF2 to a CYLD mutant mimicking phosphorylation on Ser 418 is not affected."
AZI2 affects CXCL8, CYLD, DDX3X, DDX58, DHX58, IFIH1, IL12A, IL12B, IRF7, ISG15, MAPK11, NFKB1, NFKBIA, RELA, RIPK1, TANK, TBK1, TNF, TRAF2, and TRIM25
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