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PMID: 16982211 The binding of TNF to TNF receptor-1 (TNF-R1; the main receptor for soluble TNF on most cell types) (A) leads to the recruitment of TNF receptor-1 associated death domain protein (TRADD; red), which in turn recruits TNF receptor-associated factor 2 (TRAF2; orange) and receptor-interacting protein (RIP; dark grey). PMID: 16982211 The binding of TNF to TNF receptor-1 (TNF-R1; the main receptor for soluble TNF on most cell types) (A) leads to the recruitment of TNF receptor-1 associated death domain protein (TRADD; red), which in turn recruits TNF receptor-associated factor 2 (TRAF2; orange) and receptor-interacting protein (RIP; dark grey). PMID: 16982211 After its Ub ligase activity is turned on, TRAF2 catalyses K63 polyubiquitination of itself (A1). PMID: 16982211 This causes the release of TRAF2 into the cytosol and TRAF2-mediated K63 polyubiqutination of RIP (A2). PMID: 16982211 This causes the release of TRAF2 into the cytosol and TRAF2-mediated K63 polyubiqutination of RIP (A2). PMID: 16982211 K63 polyubiquitinated RIP is recognized by the TAK1-binding proteins TAB2 and TAB3 (blue), as well as by IkappaB kinase gamma (IKKgamma; light green). PMID: 16982211 This brings the kinase TAK1 (light grey) in close proximity to the IKK complex, allowing it to phosphorylate the catalytic IKKalpha and IKKbeta subunits (pink; A3). PMID: 16982211 This brings the kinase TAK1 (light grey) in close proximity to the IKK complex, allowing it to phosphorylate the catalytic IKKalpha and IKKbeta subunits (pink; A3). PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The binding of IL-1beta to the IL-1 receptor (IL-1R)–IL-1R accessory protein (IL-1RAcP) complex (B), or the binding of lipopolysaccharide (LPS) to the TLR4–MD2–CD14 complex (C), leads to the recruitment of myeloid differentiation factor 88 (MyD88; light yellow) and MyD88 adaptor-like (MAL), which subsequently recruit IL-1 receptor-associated kinase 1 (IRAK1; green), IRAK4 (purple) and TRAF6 (dark blue) to the receptor complex. PMID: 16982211 The phosphorylation of IRAK1 by IRAK4 (B1, C1) leads to the hyperphosphorylation of IRAK1 (B2, C2), followed by the dissociation of the IRAK1–TRAF6 complex from the receptor. PMID: 16982211 The phosphorylation of IRAK1 by IRAK4 (B1, C1) leads to the hyperphosphorylation of IRAK1 (B2, C2), followed by the dissociation of the IRAK1–TRAF6 complex from the receptor. PMID: 16982211 The phosphorylation of IRAK1 by IRAK4 (B1, C1) leads to the hyperphosphorylation of IRAK1 (B2, C2), followed by the dissociation of the IRAK1–TRAF6 complex from the receptor. PMID: 16982211 The phosphorylation of IRAK1 by IRAK4 (B1, C1) leads to the hyperphosphorylation of IRAK1 (B2, C2), followed by the dissociation of the IRAK1–TRAF6 complex from the receptor. PMID: 16982211 Once released from the receptor, the Ub-ligase activity of TRAF6 mediates its K63 auto-polyubiquitination (BC3). PMID: 16982211, 16543409 This is further supported by the finding that overexpression of SOCS3 inhibits IL-1-induced NF-kappaB activation and co-immunoprecipitates with the TRAF6–TAK1 complex. PMID: 16982211 K63-polyubiquitinated TRAF6 then recruits the TAK1–TAB2–TAB3 complex, which subsequently phosphorylates and activates IKKalpha and IKKbeta (BC4). Indirect PMID: 16982211 K63-polyubiquitinated TRAF6 then recruits the TAK1–TAB2–TAB3 complex, which subsequently phosphorylates and activates IKKalpha and IKKbeta (BC4). PMID: 16982211 The IKKbeta catalytic subunit then phosphorylates the inhibitor of kappaB (IkappaB)α protein (D1), which keeps NF-kappaB (shown here as a p65–p50 dimer) in the cytoplasm of resting cells. PMID: 16982211 IkappaBalpha phosphorylation leads to its K48 polyubiquitination (D2) and subsequent proteasomal degradation (D3). PMID: 16982211 IkappaBalpha phosphorylation leads to its K48 polyubiquitination (D2) and subsequent proteasomal degradation (D3). PMID: 16982211, 16214042 Recently, ubiquitin specific peptidase 31 (USP31) was identified as another TRAF2 binding DUB that inhibits TNF-induced NF-kappaB activation upon overexpression. PMID: 16982211, 8557994, 11463333, 16204640 Interestingly, overexpression of these genes was shown to inhibit TNF-induced and IL-1-induced NF-kappaB activation. PMID: 16982211, 16543409 This is further supported by the finding that overexpression of SOCS3 inhibits IL-1-induced NF-kappaB activation and co-immunoprecipitates with the TRAF6–TAK1 complex. PMID: 16982211 This allows NF-kappaB to translocate to the nucleus (D4), where it induces the transcription of genes with an NF-kappaB consensus site in their promoter region, including IkappaBalpha. PMID: 16982211 This allows NF-kappaB to translocate to the nucleus (D4), where it induces the transcription of genes with an NF-kappaB consensus site in their promoter region, including IkappaBalpha. PMID: 16982211 This allows NF-kappaB to translocate to the nucleus (D4), where it induces the transcription of genes with an NF-kappaB consensus site in their promoter region, including IkappaBalpha. PMID: 16982211 This newly synthesized IκBα can establish a negative-feedback loop by moving to the nucleus (D5), where it removes DNA-bound NF-kappaB complexes from their cognate sites and exports them back to the cytoplasm (D6). Indirect PMID: 16982211 This newly synthesized IκBα can establish a negative-feedback loop by moving to the nucleus (D5), where it removes DNA-bound NF-kappaB complexes from their cognate sites and exports them back to the cytoplasm (D6). PMID: 16982211 This newly synthesized IκBα can establish a negative-feedback loop by moving to the nucleus (D5), where it removes DNA-bound NF-kappaB complexes from their cognate sites and exports them back to the cytoplasm (D6). PMID: 16982211 This newly synthesized IκBα can establish a negative-feedback loop by moving to the nucleus (D5), where it removes DNA-bound NF-kappaB complexes from their cognate sites and exports them back to the cytoplasm (D6). PMID: 16982211 This newly synthesized IκBα can establish a negative-feedback loop by moving to the nucleus (D5), where it removes DNA-bound NF-kappaB complexes from their cognate sites and exports them back to the cytoplasm (D6). PMID: 16982211 TLR-induced activation of NF-kappaB leads to the expression of several NF-kappaB-dependent genes, including cytokines such as tumor necrosis factor (TNF) and interleukin (IL)-1beta, both of which also directly activate the NF-kappaB pathway and thus establish a positive autoregulatory loop. PMID: 16982211 TLR-induced activation of NF-kappaB leads to the expression of several NF-kappaB-dependent genes, including cytokines such as tumor necrosis factor (TNF) and interleukin (IL)-1beta, both of which also directly activate the NF-kappaB pathway and thus establish a positive autoregulatory loop. PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. Indirect PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. Indirect PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. Indirect PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. Indirect PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. Indirect PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. Indirect PMID: 16982211, 12360211 This simultaneous and well-orchestrated activation of NF-kappaB by PAMPs and pro-inflammatory cytokines leads to the production of NF-kappaB-dependent chemokines (e.g. IL-8 and eotaxin), adhesion molecules (e.g. E-selectin and intercellular adhesion molecule 1) and inducible enzymes (e.g. inducible nitric oxide synthase and cyclo-oxygenase-2), all of which contribute to the strength and duration of the inflammatory response. Indirect PMID: 16982211, 8557994, 8692885 Because overexpression of A20 was shown to inhibit NF-kappaB activation in response to many stimuli including TNF and IL-1 19 and 20, it was originally suggested that A20 is a feedback inhibitor of NF-kappaB signalling. PMID: 16982211, 8557994, 11463333, 16204640 Interestingly, overexpression of these genes was shown to inhibit TNF-induced and IL-1-induced NF-kappaB activation. Indirect PMID: 16982211, 8557994, 8692885 Because overexpression of A20 was shown to inhibit NF-kappaB activation in response to many stimuli including TNF and IL-1 19 and 20, it was originally suggested that A20 is a feedback inhibitor of NF-kappaB signalling. PMID: 16982211, 8557994, 11463333, 16204640 Interestingly, overexpression of these genes was shown to inhibit TNF-induced and IL-1-induced NF-kappaB activation. Indirect PMID: 16982211, 15334086, 15258597, 15653317 It was subsequently demonstrated that A20 can disassemble K63 polyubiquitin chains from RIP and TRAF6 in the TNF-receptor-induced and TLR4 [lipopolysaccharide (LPS)]-induced NF-kappaB signalling pathway, respectively. PMID: 16982211, 15334086, 15258597, 15653317 It was subsequently demonstrated that A20 can disassemble K63 polyubiquitin chains from RIP and TRAF6 in the TNF-receptor-induced and TLR4 [lipopolysaccharide (LPS)]-induced NF-kappaB signalling pathway, respectively. PMID: 16982211, 15258597, 15653317 The de-ubiquitinating and Ub-conjugating activities of A20 are ordered in two steps: the N-terminal OTU domain of A20 first removes the K63-linked polyubiquitin chains from RIP and inactivates it, and the C-terminal zinc finger domain of A20 catalyses K48 polyubiquitination of RIP, thereby targeting it for proteasomal degradation. PMID: 16982211, 16684768 Recently, TNF-induced IKKgamma ubiquitination was also reported to be sensitive to A20-mediated de-ubiquitination, indicating that A20 might act at different levels of the NF-kappaB signalling pathway. Indirect PMID: 16982211, 16684768 Recently, TNF-induced IKKgamma ubiquitination was also reported to be sensitive to A20-mediated de-ubiquitination, indicating that A20 might act at different levels of the NF-kappaB signalling pathway. PMID: 16982211, 11463333, 12682062 One of them is OTUD7B (also known as Cezanne), which interacts with TRAF6 and inhibits NF-kappaB activation upon overexpression. Indirect Indirect Indirect PMID: 16982211, 12917690, 12917691, 12917689 Overexpression of CYLD interferes with IKK activation by catalysing the selective cleavage of K63 polyubiquitin chains from TRAF2 and TRAF6, consistent with its inhibitory effect on both TNF-receptor- and TLR–IL-1-receptor-initiated NF-kappaB activation. PMID: 16982211, 11907583, 12411493 For example, the TNF-induced recruitment of TRAF2 to TNF receptor-1 (the main receptor for soluble TNF on most cell types) and TNF receptor-2 (the main receptor for membrane-bound TNF, and primarily expressed on T cells) is followed by TRAF2 ubiquitination by two RING finger Ub ligases: baculoviral IAP repeat-containing 2 (BIRC2; also known as cIAP1) and seven in absentia homolog 2 (SIAH2). Indirect PMID: 16982211, 12917690, 12917691, 12917689 Overexpression of CYLD interferes with IKK activation by catalysing the selective cleavage of K63 polyubiquitin chains from TRAF2 and TRAF6, consistent with its inhibitory effect on both TNF-receptor- and TLR–IL-1-receptor-initiated NF-kappaB activation. PMID: 16982211, 16543409 Instead, SOCS3 decreased TRAF6 polyubiquitination, thus preventing the association and activation of TAK1. PMID: 16982211, 16230348, 15226292 Moreover, endogenous expression of CYLD is upregulated by TNF, IL-1 and TLR2 ligands in an NF-kappaB-dependent way, supporting a negative-feedback role for CYLD in the NF-kappaB pathway. PMID: 16982211, 16713561 For example, CYLD was recently shown to de-ubiquitinate B-cell CLL/lymphoma 3 (BCL3), preventing its nuclear translocation. Indirect PMID: 16982211, 16713561 For example, CYLD was recently shown to de-ubiquitinate B-cell CLL/lymphoma 3 (BCL3), preventing its nuclear translocation. PMID: 16982211, 16713561 For example, CYLD was recently shown to de-ubiquitinate B-cell CLL/lymphoma 3 (BCL3), preventing its nuclear translocation. PMID: 16982211, 16214042 Recently, ubiquitin specific peptidase 31 (USP31) was identified as another TRAF2 binding DUB that inhibits TNF-induced NF-kappaB activation upon overexpression. PMID: 16982211, 15107846 In this context, the RING finger containing Ub ligase Triad3A was shown to bind and induce the ubiquitination and degradation of TLR4 and TLR9, but not TLR2. PMID: 16982211, 15107846 In this context, the RING finger containing Ub ligase Triad3A was shown to bind and induce the ubiquitination and degradation of TLR4 and TLR9, but not TLR2. PMID: 16982211, 15107846 In this context, the RING finger containing Ub ligase Triad3A was shown to bind and induce the ubiquitination and degradation of TLR4 and TLR9, but not TLR2. PMID: 16982211, 15107846 In this context, the RING finger containing Ub ligase Triad3A was shown to bind and induce the ubiquitination and degradation of TLR4 and TLR9, but not TLR2. PMID: 16982211, 15107846 In this context, the RING finger containing Ub ligase Triad3A was shown to bind and induce the ubiquitination and degradation of TLR4 and TLR9, but not TLR2. PMID: 16982211, 15107846 In this context, the RING finger containing Ub ligase Triad3A was shown to bind and induce the ubiquitination and degradation of TLR4 and TLR9, but not TLR2. PMID: 16982211, 15899873 In addition, TNF-receptor-2 plasma-membrane levels are regulated by TNF-induced K48 polyubiquitination mediated by Ankyrin repeat and SOCS box-containing 3 (ASB3), which confers its Ub-ligase activity via an interaction with elongin B–elongin C and the recruitment of the Ub-transferase system composed of cullin-2, Rbx2 and E2. PMID: 16982211 SOCS proteins are characterized by a C-terminal SOCS-box domain that allows the binding of the elongin-B–elongin-C complex to form a functional E3 Ub ligase. Indirect PMID: 16982211, 15899873 In addition, TNF-receptor-2 plasma-membrane levels are regulated by TNF-induced K48 polyubiquitination mediated by Ankyrin repeat and SOCS box-containing 3 (ASB3), which confers its Ub-ligase activity via an interaction with elongin B–elongin C and the recruitment of the Ub-transferase system composed of cullin-2, Rbx2 and E2. PMID: 16982211, 11907583, 12411493 For example, the TNF-induced recruitment of TRAF2 to TNF receptor-1 (the main receptor for soluble TNF on most cell types) and TNF receptor-2 (the main receptor for membrane-bound TNF, and primarily expressed on T cells) is followed by TRAF2 ubiquitination by two RING finger Ub ligases: baculoviral IAP repeat-containing 2 (BIRC2; also known as cIAP1) and seven in absentia homolog 2 (SIAH2). PMID: 16982211, 11907583, 12411493 For example, the TNF-induced recruitment of TRAF2 to TNF receptor-1 (the main receptor for soluble TNF on most cell types) and TNF receptor-2 (the main receptor for membrane-bound TNF, and primarily expressed on T cells) is followed by TRAF2 ubiquitination by two RING finger Ub ligases: baculoviral IAP repeat-containing 2 (BIRC2; also known as cIAP1) and seven in absentia homolog 2 (SIAH2). PMID: 16982211, 11907583, 12411493 For example, the TNF-induced recruitment of TRAF2 to TNF receptor-1 (the main receptor for soluble TNF on most cell types) and TNF receptor-2 (the main receptor for membrane-bound TNF, and primarily expressed on T cells) is followed by TRAF2 ubiquitination by two RING finger Ub ligases: baculoviral IAP repeat-containing 2 (BIRC2; also known as cIAP1) and seven in absentia homolog 2 (SIAH2). Indirect PMID: 16982211, 11907583, 15861135 Binding of BIRC2 to TRAF2 at TNF receptor-2 induces the translocation of the TRAF2–BIRC2 complex to an endoplasmic-reticulum-associated compartment, where BIRC2 ubiquitinates TRAF2, thereby triggering its proteasomal degradation and the subsequent cessation of TRAF2-mediated signalling. PMID: 16982211, 11907583, 12411493 For example, the TNF-induced recruitment of TRAF2 to TNF receptor-1 (the main receptor for soluble TNF on most cell types) and TNF receptor-2 (the main receptor for membrane-bound TNF, and primarily expressed on T cells) is followed by TRAF2 ubiquitination by two RING finger Ub ligases: baculoviral IAP repeat-containing 2 (BIRC2; also known as cIAP1) and seven in absentia homolog 2 (SIAH2). PMID: 16982211, 11907583, 15861135 Binding of BIRC2 to TRAF2 at TNF receptor-2 induces the translocation of the TRAF2–BIRC2 complex to an endoplasmic-reticulum-associated compartment, where BIRC2 ubiquitinates TRAF2, thereby triggering its proteasomal degradation and the subsequent cessation of TRAF2-mediated signalling. PMID: 16982211, 11907583, 15861135 Binding of BIRC2 to TRAF2 at TNF receptor-2 induces the translocation of the TRAF2–BIRC2 complex to an endoplasmic-reticulum-associated compartment, where BIRC2 ubiquitinates TRAF2, thereby triggering its proteasomal degradation and the subsequent cessation of TRAF2-mediated signalling. Indirect PMID: 16982211, 11907583, 15861135 Binding of BIRC2 to TRAF2 at TNF receptor-2 induces the translocation of the TRAF2–BIRC2 complex to an endoplasmic-reticulum-associated compartment, where BIRC2 ubiquitinates TRAF2, thereby triggering its proteasomal degradation and the subsequent cessation of TRAF2-mediated signalling. PMID: 16982211, 12411493 Similarly, the triggering of TNF receptor-1 induces proteasomal degradation of TRAF2 upon overexpression of the E3 Ub ligase SIAH2. PMID: 16982211, 15258597, 15653317 The de-ubiquitinating and Ub-conjugating activities of A20 are ordered in two steps: the N-terminal OTU domain of A20 first removes the K63-linked polyubiquitin chains from RIP and inactivates it, and the C-terminal zinc finger domain of A20 catalyses K48 polyubiquitination of RIP, thereby targeting it for proteasomal degradation. PMID: 16982211, 8557994, 11463333, 16204640 Interestingly, overexpression of these genes was shown to inhibit TNF-induced and IL-1-induced NF-kappaB activation. PMID: 16982211, 8557994, 11463333, 16204640 Interestingly, overexpression of these genes was shown to inhibit TNF-induced and IL-1-induced NF-kappaB activation. PMID: 16982211, 8557994, 11463333, 16204640 Interestingly, overexpression of these genes was shown to inhibit TNF-induced and IL-1-induced NF-kappaB activation. PMID: 16982211, 8557994, 11463333, 16204640 Interestingly, overexpression of these genes was shown to inhibit TNF-induced and IL-1-induced NF-kappaB activation. Indirect PMID: 16982211, 16415872 Recently, it was observed that the TLR2 and TLR4 adaptor protein MyD88 adaptor-like (MAL, also known as TIRAP) is phosphorylated and ubiquitinated in a SOCS1-dependent manner upon TLR stimulation, thereby targeting MAL for proteasomal degradation. PMID: 16982211, 16415872 Recently, it was observed that the TLR2 and TLR4 adaptor protein MyD88 adaptor-like (MAL, also known as TIRAP) is phosphorylated and ubiquitinated in a SOCS1-dependent manner upon TLR stimulation, thereby targeting MAL for proteasomal degradation. Indirect PMID: 16982211, 16415872 Recently, it was observed that the TLR2 and TLR4 adaptor protein MyD88 adaptor-like (MAL, also known as TIRAP) is phosphorylated and ubiquitinated in a SOCS1-dependent manner upon TLR stimulation, thereby targeting MAL for proteasomal degradation. Indirect PMID: 16982211, 12433373, 14690596 Indeed, an interaction of SOCS1 with IRAK1 as well as SOCS1-mediated ubiquitination and subsequent degradation of the p65 NF-κB subunit suggest a more downstream inhibitory effect of SOCS1 in TLR signalling pathways. Indirect PMID: 16982211, 12433373, 14690596 Indeed, an interaction of SOCS1 with IRAK1 as well as SOCS1-mediated ubiquitination and subsequent degradation of the p65 NF-κB subunit suggest a more downstream inhibitory effect of SOCS1 in TLR signalling pathways. PMID: 16982211, 12433373, 14690596 Indeed, an interaction of SOCS1 with IRAK1 as well as SOCS1-mediated ubiquitination and subsequent degradation of the p65 NF-κB subunit suggest a more downstream inhibitory effect of SOCS1 in TLR signalling pathways. PMID: 16982211, 16543409 This is further supported by the finding that overexpression of SOCS3 inhibits IL-1-induced NF-kappaB activation and co-immunoprecipitates with the TRAF6–TAK1 complex. PMID: 16982211, 16543409 This is further supported by the finding that overexpression of SOCS3 inhibits IL-1-induced NF-kappaB activation and co-immunoprecipitates with the TRAF6–TAK1 complex. PMID: 16982211, 16543409 Instead, SOCS3 decreased TRAF6 polyubiquitination, thus preventing the association and activation of TAK1.