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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-κB 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-κB 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-κB 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-κB, 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-κB, 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-κB, 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