IndraLab

Statements

CYLD binds IKBKG. 49 / 50
11 1 | 23 14
reach
"NEMO, another potential adaptor of CYLD, directly binds CYLD and associates with various IKK regulators, such as RIP1 and TRAF2 [XREF_BIBR]."
28031783
sparser
"Interestingly, the association of CYLD with IKKγ coincides with the appearance of a phosphorylated form of CYLD, though it has not been shown that this modification is required for interaction and deubiquitinating activities xref ."
24586659
biogrid
No evidence text available
12917691
reach
"Three independent studies have recently shown that CYLD binds to NEMO and facilitates the disassembly of K63 linked polyubiquitin chains on TRAF2, TRAF6 and NEMO [22 ** -24 **]."
15196553
reach
"However, the SUMOylation effectively impairs the interaction between NEMO and CYLD, suggesting that the SUMO-moiety (~ 12 kDa) might directly mask the binding surface."
23825957
sparser
"Strikingly, GST-CYLD (470–684 aa) could pull down neither the NEMO-SUMO-3 nor the SUMOylated NEMO ( xref , left panel and xref ), whereas GST-IKKβ (644–756 aa) could pull down both the NEMO-SUMO-3 and the SUMOylated NEMO ( xref , right panel and xref ), indicating that the SUMO-3 modification specifically impaired the interaction between NEMO and CYLD."
23825957
reach
"Removal of Lys-63-chains from TRAFs requires that CYLD physically (and transiently) interact with NEMO, e.g. in response to TNF-alpha stimulation."
20347313
biogrid
No evidence text available
21988832
reach
"For example, CYLD directly associates and deubiquitinates NEMO and TRAF-6, thus inhibiting TNF-alpha-induced nuclear factor-kappaB (NF-kappaB) signaling [13,15-17]."
26056944
sparser
"Following TLR signaling, NF-κB essential modifier (NEMO/IKKγ) undergoes SUMO-2/3 modification, which prevents NEMO binding to the deubiquitinase CYLD and thus indirectly enhancing the IKK activation."
34336833
reach
"CYLD interacts with NEMO and is phosphorylated by IKK as a mechanism to inactivate CYLD DUB activity."
22435550
biogrid
No evidence text available
12917691
reach
"NEMO is a target for both SUMOylation and ubiquitination, and how NEMO SUMOylation affects the binding of NEMO with deubiquitinase CYLD and thus the activation of the NF-κB pathway is relatively unclear.TLR-dependent NF-κB activation is mediated by the TAK1 signalosome consisting of the TRAF6/TAB2/TAK1 complex."
34336833
reach
"Interestingly, CYLD interacts with NEMO and TRAF2, both of which are recruited to the TNF receptor upon ligand binding."
14676304
reach
"Mechanistically, CYLD binds to NEMO and TRAF2 and reverses non-K48-linked polyubiquitination of TRAF2, thereby blocking TRAF2 mediated activation of the IKK complex [XREF_BIBR - XREF_BIBR] (XREF_FIG)."
27844253
reach
"Indeed, IKKgamma binds CYLD as well as the catalytic subunits of IKK [XREF_BIBR]."
24928390
sparser
"Indeed, knockdown of SENP6 impaired the endogenous association of NEMO and CYLD ( xref )."
23825957
reach
"Another potential adaptor of CYLD is NEMO, which directly binds CYLD and associates with various IKK regulators, such as RIP1 and TRAF2."
19373246
reach
"NEMO is a target for both SUMOylation and ubiquitination, and how NEMO SUMOylation affects the binding of NEMO with deubiquitinase CYLD and thus the activation of the NF-kappaB pathway is relatively unclear."
34336833
reach
"NEMO is a target for both SUMOylation and ubiquitination, and how NEMO SUMOylation affects the binding of NEMO with deubiquitinase CYLD and thus the activation of the NF-κB pathway is relatively unclear."
34336833
biogrid
No evidence text available
22990857
sparser
"CYLD interacts with NEMO, TNF receptor-associated factor (TRAF)-2, and TRAF-interacting protein and negatively regulates the canonical NF- κ B signal transduction pathway ( Brummelkamp et al. , 2003 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17851586
sparser
"CYLD interacts with NEMO and is phosphorylated by IKK as a mechanism to inactivate CYLD DUB activity ( xref )."
22435550
reach
"As previously mentioned CYLD can bind to NEMO and NF-kappaB that have been identified as its substrates."
27597804
reach
"CYLD interacts with NEMO, TNF receptor associated factor (TRAF)-2, and TRAF interacting protein and negatively regulates the canonical NF- kappa B signal transduction pathway (Brummelkamp et al., 2003[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
17851586
reach
"We show that CYLD binds to the NEMO (also known as IKKgamma) component of the IkappaB kinase (IKK) complex, and appears to regulate its activity through de-ubiquitination of TRAF2, as TRAF2 ubiquitination can be modulated by CYLD."
12917690
reach
"Previous studies reported that CYLD binds to IKKgamma and its upstream signaling components including TAK1, TRAF2, TRAF6, and RIP1 [XREF_BIBR - XREF_BIBR]."
29259980
biogrid
No evidence text available
16627981
sparser
"NEMO is a target for both SUMOylation and ubiquitination, and how NEMO SUMOylation affects the binding of NEMO with deubiquitinase CYLD and thus the activation of the NF-κB pathway is relatively unclear."
34336833
biogrid
No evidence text available
12917690
sparser
"Three independent studies have recently shown that CYLD binds to NEMO and facilitates the disassembly of K63-linked polyubiquitin chains on TRAF2, TRAF6 and NEMO [22 •• –24 •• ] ."
15196553
sparser
"Another potential adaptor of CYLD is NEMO, which directly binds CYLD and associates with various IKK regulators, such as RIP1 and TRAF2."
19373246
sparser
"Indeed, IKKγ binds CYLD as well as the catalytic subunits of IKK [ xref ]."
24928390
hprd
No evidence text available
15341735
reach
"Recently, it was reported that CYLD directly interacts with NEMO and IKKgamma and TRAF2 in the NF-kappaB signaling pathway."
15341735
sparser
"CYLD associates with zinc-finger of NEMO, cleaves non-K48-linked poly-ubiquitin chains attached to NEMO, and negatively modulates TRAF-mediated activation of IKK xref ."
26240016
sparser
"Removal of Lys-63-chains from TRAFs requires that CYLD physically (and transiently) interact with NEMO, e.g. in response to TNF-α stimulation."
20347313
reach
"Notably, the deubiquitinase CYLD could interact with NEMO and cleave these polyubiquitin chains, thus acting as a negative regulator of NF-kappaB signaling XREF_BIBR."
23825957
biogrid
No evidence text available
12917691
biogrid
No evidence text available
26802121
biogrid
No evidence text available
26802121
biogrid
No evidence text available
12917691
biogrid
No evidence text available
12917689
reach
"CYLD physically interacts with and deubiquitinates NEMO, thereby negatively regulating NF-kappaB activation [XREF_BIBR]."
18775672
sparser
"However, the SUMOylation effectively impairs the interaction between NEMO and CYLD, suggesting that the SUMO-moiety (∼12 kDa) might directly mask the binding surface."
23825957
reach
"In cells, CYLD reportedly interacts with both NEMO and IKKgamma and TRAF (Brummelkamp et al., 2003; Kovalenko et al., 2003; Trompouki et al., 2003); however, it is unlikely that only CYLD links NEMO a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
15341735
sparser
"CYLD binding to NEMO is indeed required for its phosphorylation by the IKK complex, which in turn inhibits its DUB activity, leading to NF-κB activation xref ."
21448225
reach
"Strikingly, GST-CYLD (470-684 aa) could pull down neither the NEMO-SUMO-3 nor the SUMOylated NEMO (XREF_FIG, left panel and XREF_FIG), whereas GST-IKKbeta (644-756 aa) could pull down both the NEMO-SUMO-3 and the SUMOylated NEMO (XREF_FIG, right panel and XREF_FIG), indicating that the SUMO-3 modification specifically impaired the interaction between NEMO and CYLD."
23825957
reach
"Here we report that CYLD, a tumour suppressor that is mutated in familial cylindromatosis, interacts with NEMO, the regulatory subunit of IKK."
12917691