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indirect
indirect
PMID: 15809659,12591926
TRAF2 and TRAF5 also contain a RING domain and UbLys63 modifications can be detected in TRAF2 on TNF-alpha stimulation
indirect
PMID: 15809659,15258597
In addition, TRAF2 catalyses Lys 63 polyubiquitination of receptor-interacting protein (RIP)
indirect
PMID: 15809659,12591926,11460167
Both TRAF2 and TRAF6 activate c-Jun amino-terminal kinase (JNK) in parallel to IKK, in a process that also depends on the assembly of UbLys63 chains
PMID: 15809659
Figure 2A
PMID: 15809659
Ubiquitin (Ub) ligases (shown in green) catalyse the assembly of UbLys63 chains (green) on TRAF2, TRAF6, RIP and IKK-gamma, which is thought to recruit the protein kinase TAK1 through association with TAB2 or TAB3.
PMID: 15809659
Figure 2A
PMID: 15809659
Ubiquitin (Ub) ligases (shown in green) catalyse the assembly of UbLys63 chains (green) on TRAF2, TRAF6, RIP and IKK-gamma, which is thought to recruit the protein kinase TAK1 through association with TAB2 or TAB3.
indirect
indirect
PMID: 15809659,10215628
Genetic ablation has demonstrated an essential function of TRAF6 in IKK activation through IL-1 receptor (IL-1R) and Toll-like receptor (TLR) signalling
PMID: 15809659,11460167
TRAF6 undergoes trans-auto-ubiquitination , which is strongly enhanced by its forced oligomerization
PMID: 15809659
Figure 2A
indirect
indirect
PMID: 15809659,10215628
Genetic ablation has demonstrated an essential function of TRAF6 in IKK activation through IL-1 receptor (IL-1R) and Toll-like receptor (TLR) signalling
PMID: 15809659,11460167
TRAF6 undergoes trans-auto-ubiquitination , which is strongly enhanced by its forced oligomerization
PMID: 15809659
Figure 2A
indirect
PMID: 15809659,11460167
TRAF6 undergoes trans-auto-ubiquitination , which is strongly enhanced by its forced oligomerization
PMID: 15809659,15492226
TRAF-interacting protein with forkhead-associated domain (TIFA) oligomers promote TRAF6 oligomerization and Ub ligase activity
PMID: 15809659,11460167
TRAF6 undergoes trans-auto-ubiquitination , which is strongly enhanced by its forced oligomerization
PMID: 15809659,15492226
TRAF-interacting protein with forkhead-associated domain (TIFA) oligomers promote TRAF6 oligomerization and Ub ligase activity
PMID: 15809659,12591926,11460167
Both TRAF2 and TRAF6 activate c-Jun amino-terminal kinase (JNK) in parallel to IKK, in a process that also depends on the assembly of UbLys63 chains
PMID: 15809659
Figure 2A
PMID: 15809659
Ubiquitin (Ub) ligases (shown in green) catalyse the assembly of UbLys63 chains (green) on TRAF2, TRAF6, RIP and IKK-gamma, which is thought to recruit the protein kinase TAK1 through association with TAB2 or TAB3.
indirect
PMID: 15809659
TAK1 activates the IKK complex, which subsequently targets IkappaBs for BetaTrCP-mediated UbLys48 modification.
PMID: 15809659
Figure 2A
indirect
PMID: 15809659
TAK1 activates the IKK complex, which subsequently targets IkappaBs for BetaTrCP-mediated UbLys48 modification.
PMID: 15809659
Figure 2A
indirect
PMID: 15809659
TAK1 activates the IKK complex, which subsequently targets IkappaBs for BetaTrCP-mediated UbLys48 modification.
PMID: 15809659
Figure 2A
indirect
PMID: 15809659
Figure 2A
indirect
PMID: 15809659
Figure 2A
indirect
PMID: 15809659
TAK1 activates the IKK complex, which subsequently targets IkappaBs for BetaTrCP-mediated UbLys48 modification.
indirect
PMID: 15809659
Figure2A
PMID: 15809659
Figure2A
PMID: 15809659,15122200
T-cell receptor (TCR) ligation triggers protein kinase Cdelta (PKCdelta)-mediated formation of a complex that consists of the CARMA1 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 1), B-cell lymphoma 10 (BCL10) and mucosa-associated lymphoid tissue (MALT1) proteins and transmits the signal to the IKK complex
indirect
MID: 15809659,15122200
T-cell receptor (TCR) ligation triggers protein kinase Cdelta (PKCdelta)-mediated formation of a complex that consists of the CARMA1 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 1), B-cell lymphoma 10 (BCL10) and mucosa-associated lymphoid tissue (MALT1) proteins and transmits the signal to the IKK complex
indirect
PMID: 15809659,15125833
BCL10 and MALT1 can induce E3 activity of TRAF6, and RNA interference (RNAi) suggests that TRAF2 and TRAF6 are necessary for IKK activation in Jurkat T cells after TCR ligation
indirect
PMID: 15809659,11262391
BCL10 induces oligomerization of MALT1 which might enhance its Ub ligase activity.
indirect
PMID: 15809659,14695475
MALT1 triggers UbLys63 modification of Lys 399 in the carboxy-terminal zinc-finger domain of IKKgamma; mutation of this residue abolishes IKK/NF-KappaB activation by BCL10
PMID: 15809659,15620648
Nucleotide-binding oligomerization domain 2 (NOD2), which functions as an intracellular sensor for bacteria, promotes RIP2-dependent NF-ÎşB activation by inducing the assembly of Lys 63 polyUb chains at position Lys 285 of IKKgamma
indirect
indirect
PMID: 15809659,15620648
Nucleotide-binding oligomerization domain 2 (NOD2), which functions as an intracellular sensor for bacteria, promotes RIP2-dependent NF-ÎşB activation by inducing the assembly of Lys 63 polyUb chains at position Lys 285 of IKKgamma
indirect
PMID: 15809659,15620648
Nucleotide-binding oligomerization domain 2 (NOD2), which functions as an intracellular sensor for bacteria, promotes RIP2-dependent NF-ÎşB activation by inducing the assembly of Lys 63 polyUb chains at position Lys 285 of IKKgamma
indirect
PMID: 15809659,15226292
Expression of CYLD is induced by NF-KappaB, which provides a novel autoregulatory feedback pathway that could limit the duration of IKK activity
indirect
PMID: 15809659,12917690,12917691,12917689
CYLD interferes with IKK/NF-KappaB signalling by catalysing the selective cleavage of UbLys63 chains from TRAF2, TRAF6 and IKKgamma, without affecting UbLys48-modified IKappaBalpha or Beta-catenin
indirect
PMID: 15809659,12917690,12917691,12917689
CYLD interferes with IKK/NF-KappaB signalling by catalysing the selective cleavage of UbLys63 chains from TRAF2, TRAF6 and IKKgamma, without affecting UbLys48-modified IKappaBalpha or Beta-catenin
PMID: 15809659,12917690,12917691,12917689
CYLD interferes with IKK/NF-KappaB signalling by catalysing the selective cleavage of UbLys63 chains from TRAF2, TRAF6 and IKKgamma, without affecting UbLys48-modified IKappaBalpha or Beta-catenin
indirect
PMID: 15809659
Figure 2A
PMID: 15809659,10983987
The ubiquitin-like PLIC may provide a link between the ubiquitination machinery and the proteasome
indirect
PMID: 15809659
Overexpression of CYLD represses NF-KappaB activation in response to various stimuli, including TNF and IL-1.
indirect
PMID: 15809659
Overexpression of CYLD represses NF-KappaB activation in response to various stimuli, including TNF and IL-1.
indirect
PMID: 15809659,15334086,15258597
The N-terminal ovarian tumour (OTU) domain of A20 contains DUB activity and catalyses the removal of UbLys63 chains from RIP and TRAF6, thereby interfering with TNFR and TLR signalling to IKKs/NF-KappaB, respectively
indirect
PMID: 15809659,15334086,15258597
The N-terminal ovarian tumour (OTU) domain of A20 contains DUB activity and catalyses the removal of UbLys63 chains from RIP and TRAF6, thereby interfering with TNFR and TLR signalling to IKKs/NF-KappaB, respectively
indirect
indirect
PMID: 15809659,15258597
Subsequently, the C-terminal zinc-finger domain functions as a Ub ligase that mediates UbLys48 modification of RIP and initiates its proteasomal degradation
PMID: 15809659
Figure2B
PMID: 15809659,12753742,15258597
Binding of TNF-alpha to TNFRI induces ubiquitination and degradation of RIP after recruitment to lipid rafts with A20 acting as the potential Ub ligase in this reaction
PMID: 15809659,15258597
Subsequently, the C-terminal zinc-finger domain functions as a Ub ligase that mediates UbLys48 modification of RIP and initiates its proteasomal degradation
PMID: 15809659
Figure2B
PMID: 15809659,11907583
TNFRII-dependent process that requires the cellular inhibitor of apoptosis protein (c-IAP1) as a Ub ligase, TRAF2 is polyubiquitinated and degraded as well
PMID: 15809659,11463333
Using sequence similarity, Cezanne and TRAF-binding domain (TRABID) have been isolated as two further potential DUBs that contain OTU domains and can interact with TRAF6
PMID: 15809659,11463333
Using sequence similarity, Cezanne and TRAF-binding domain (TRABID) have been isolated as two further potential DUBs that contain OTU domains and can interact with TRAF6
PMID: 15809659
Ectopic expression of Cezanne downregulates NF-ÎşB, which suggests that Cezanne interferes with IKK activation
PMID: 15809659,12753742,15258597
Binding of TNF-alpha to TNFRI induces ubiquitination and degradation of RIP after recruitment to lipid rafts with A20 acting as the potential Ub ligase in this reaction
indirect
indirect
PMID: 15809659,11907583
TNFRII-dependent process that requires the cellular inhibitor of apoptosis protein (c-IAP1) as a Ub ligase, TRAF2 is polyubiquitinated and degraded as well
indirect
indirect
PMID: 15809659,11907583
TNFRII-dependent process that requires the cellular inhibitor of apoptosis protein (c-IAP1) as a Ub ligase, TRAF2 is polyubiquitinated and degraded as well
PMID: 15809659
Figure 2B
PMID: 15809659,11907583
TNFRII-dependent process that requires the cellular inhibitor of apoptosis protein (c-IAP1) as a Ub ligase, TRAF2 is polyubiquitinated and degraded as well
indirect
PMID: 15809659
Both gene products, A20 and c-IAP1, are upregulated by NF-ÎşB, which indicates that an autoregulatory circuit shuts down TNF signalling in a post-inductive manner.
indirect
PMID: 15809659
Both gene products, A20 and c-IAP1, are upregulated by NF-ÎşB, which indicates that an autoregulatory circuit shuts down TNF signalling in a post-inductive manner.
indirect
PMID: 15809659
Itch, the Ub ligase homologue to the E6-AP C-terminal (HECT) domain, and the closely related Nedd4 protein promote ubiquitination and degradation of phospholipase Cgamma1 (PLCgamma1) and PKCdelta, both of which are essential mediators of IKK/NF-KappaB activation in T cells.
indirect
PMID: 15809659
Itch, the Ub ligase homologue to the E6-AP C-terminal (HECT) domain, and the closely related Nedd4 protein promote ubiquitination and degradation of phospholipase Cgamma1 (PLCgamma1) and PKCdelta, both of which are essential mediators of IKK/NF-KappaB activation in T cells.
indirect
PMID: 15809659
Itch, the Ub ligase homologue to the E6-AP C-terminal (HECT) domain, and the closely related Nedd4 protein promote ubiquitination and degradation of phospholipase Cgamma1 (PLCgamma1) and PKCdelta, both of which are essential mediators of IKK/NF-KappaB activation in T cells.
PMID: 15809659
Itch, the Ub ligase homologue to the E6-AP C-terminal (HECT) domain, and the closely related Nedd4 protein promote ubiquitination and degradation of phospholipase Cgamma1 (PLCgamma1) and PKCdelta, both of which are essential mediators of IKK/NF-KappaB activation in T cells.
indirect
PMID: 15809659
Itch, the Ub ligase homologue to the E6-AP C-terminal (HECT) domain, and the closely related Nedd4 protein promote ubiquitination and degradation of phospholipase Cgamma1 (PLCgamma1) and PKCdelta, both of which are essential mediators of IKK/NF-KappaB activation in T cells.
PMID: 15809659
Itch, the Ub ligase homologue to the E6-AP C-terminal (HECT) domain, and the closely related Nedd4 protein promote ubiquitination and degradation of phospholipase Cgamma1 (PLCgamma1) and PKCdelta, both of which are essential mediators of IKK/NF-KappaB activation in T cells.
indirect
indirect
PMID: 15809659,15082780
Similarly, BCL10, which is downstream of PKCθ on the route to IKKs, is modified by ubiquitination and subsequently degraded after TCR/CD28 costimulation of T cells
PMID: 15809659,15082780
Similarly, BCL10, which is downstream of PKCθ on the route to IKKs, is modified by ubiquitination and subsequently degraded after TCR/CD28 costimulation of T cells
PMID: 15909659,15340068
p62 interacts through its UBA domain selectively with UbLys63-modified proteins, including TRAF6, while the N-terminal Phox and Bem1 (PB1) region provides a docking surface for the proteasome
PMID: 15909659,15340068
p62 interacts through its UBA domain selectively with UbLys63-modified proteins, including TRAF6, while the N-terminal Phox and Bem1 (PB1) region provides a docking surface for the proteasome
PMID: 15909659,15340068
p62 interacts through its UBA domain selectively with UbLys63-modified proteins, including TRAF6, while the N-terminal Phox and Bem1 (PB1) region provides a docking surface for the proteasome
PMID: 15809659,15340068
p62 interacts through its UBA domain selectively with UbLys63-modified proteins, including TRAF6, while the N-terminal Phox and Bem1 (PB1) region provides a docking surface for the proteasome
indirect
PMID: 15809659,14690596,15226358
After TNF-alpha stimulation, DNA-bound p65 is subject to ubiquitination and proteasomal degradation in the nucleus—a process that seems to be required for abrogation of NF-kappaB activity despite IKappaBalpha re-synthesis
PMID: 15809659,14690596,15226358
After TNF-alpha stimulation, DNA-bound p65 is subject to ubiquitination and proteasomal degradation in the nucleus—a process that seems to be required for abrogation of NF-kappaB activity despite IKappaBalpha re-synthesis
indirect
PMID: 15809659,14690596
It has also been shown that suppressor of cytokine signalling 1 (SOCS1) associates with p65 in LPS-treated cells; the C-terminal SOCS domain functions as an E3 ligase to catalyse the poly-ubiquitination of p65 and its subsequent degradation
PMID: 15809659,14690596
It has also been shown that suppressor of cytokine signalling 1 (SOCS1) associates with p65 in LPS-treated cells; the C-terminal SOCS domain functions as an E3 ligase to catalyse the poly-ubiquitination of p65 and its subsequent degradation
PMID: 15809659,14690596
It has also been shown that suppressor of cytokine signalling 1 (SOCS1) associates with p65 in LPS-treated cells; the C-terminal SOCS domain functions as an E3 ligase to catalyse the poly-ubiquitination of p65 and its subsequent degradation