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PMID: 18775672
This so-called canonical NF-KappaB pathway is stimulated by various immune receptors, such as the Toll-like receptors (TLRs), interleukin-1 receptor (IL-1R), tumor necrosis factor receptor (TNFR) and antigen receptors.
PMID: 18775672
The canonical pathway is activated by a large number of agonists [e.g. tumor necrosis fator (TNF), interleukin 1 (IL-1) or microbial ligands such as lipopolysaccharide (LPS)] through the triggering of various cytokine receptors or TLRs and stimulate the IKappaB kinase (IKK) complex (IKK1-IKK2-NEMO) to phosphorylate IKappaB-alpha and promote its degradation.
PMID: 18775672
The canonical pathway is activated by a large number of agonists [e.g. tumor necrosis fator (TNF), interleukin 1 (IL-1) or microbial ligands such as lipopolysaccharide (LPS)] through the triggering of various cytokine receptors or TLRs and stimulate the IKappaB kinase (IKK) complex (IKK1-IKK2-NEMO) to phosphorylate IKappaB-alpha and promote its degradation.
PMID: 18775672
This so-called canonical NF-KappaB pathway is stimulated by various immune receptors, such as the Toll-like receptors (TLRs), interleukin-1 receptor (IL-1R), tumor necrosis factor receptor (TNFR) and antigen receptors.
PMID: 18775672
The canonical pathway is activated by a large number of agonists [e.g. tumor necrosis fator (TNF), interleukin 1 (IL-1) or microbial ligands such as lipopolysaccharide (LPS)] through the triggering of various cytokine receptors or TLRs and stimulate the IKappaB kinase (IKK) complex (IKK1-IKK2-NEMO) to phosphorylate IKappaB-alpha and promote its degradation.
PMID: 18775672
This so-called canonical NF-KappaB pathway is stimulated by various immune receptors, such as the Toll-like receptors (TLRs), interleukin-1 receptor (IL-1R), tumor necrosis factor receptor (TNFR) and antigen receptors.
indirect
PMID: 18775672
On ligand engagement, each of these triggers signal transduction events that lead to the activation of the IKappaB kinase (IKK) complex, composed of two catalytic subunits (IKK1 and IKK2) and a regulatory subunit, NEMO (NF-KappaB essential modulator).
PMID: 18775672
By contrast, the canonical IKK complex triggers p105 proteolysis, which releases associated Rel subunits and also facilitates activation of the p105-associated TPL-2 MEK kinase, which triggers extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase activation
PMID: 18775672
However, p105 is phosphorylated by IKK after activation of the canonical pathway, targeting it for complete degradation by the proteasome to release associated NF-KappaB subunits.
indirect
PMID: 18775672
On ligand engagement, each of these triggers signal transduction events that lead to the activation of the IKappaB kinase (IKK) complex, composed of two catalytic subunits (IKK1 and IKK2) and a regulatory subunit, NEMO (NF-KappaB essential modulator).
indirect
PMID: 18775672
On ligand engagement, each of these triggers signal transduction events that lead to the activation of the IKappaB kinase (IKK) complex, composed of two catalytic subunits (IKK1 and IKK2) and a regulatory subunit, NEMO (NF-KappaB essential modulator).
PMID: 18775672
By contrast, the canonical IKK complex triggers p105 proteolysis, which releases associated Rel subunits and also facilitates activation of the p105-associated TPL-2 MEK kinase, which triggers extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase activation
PMID: 18775672
However, p105 is phosphorylated by IKK after activation of the canonical pathway, targeting it for complete degradation by the proteasome to release associated NF-KappaB subunits.
indirect
PMID: 18775672
Figure 1
PMID: 18775672
Activated IKK phosphorylates IKappaB-alpha, predominantly via the action of IKK2, triggering its lysine-48–linked polyubiquitination and proteasomal degradation, releasing associated NF-KappaB subunits to translocate into the nucleus.
PMID: 18775672
The canonical pathway is activated by a large number of agonists [e.g. tumor necrosis fator (TNF), interleukin 1 (IL-1) or microbial ligands such as lipopolysaccharide (LPS)] through the triggering of various cytokine receptors or TLRs and stimulate the IKappaB kinase (IKK) complex (IKK1-IKK2-NEMO) to phosphorylate IKappaB-alpha and promote its degradation.
PMID: 18775672
Activated IKK phosphorylates IKappaB-alpha, predominantly via the action of IKK2, triggering its lysine-48–linked polyubiquitination and proteasomal degradation, releasing associated NF-KappaB subunits to translocate into the nucleus
PMID: 18775672
Activated IKK phosphorylates IKappaB-alpha, predominantly via the action of IKK2, triggering its lysine-48–linked polyubiquitination and proteasomal degradation, releasing associated NF-KappaB subunits to translocate into the nucleus.
indirect
PMID:18775672
The p100-mediated pathway, often called the noncanonical NF-KappaB pathway, is triggered by a subset of TNF family members and sequentially activates NF-KappaB inducing kinase (NIK) and IKK1.
PMID: 18775672
A limited number of agonists induce processing of p100 to p52 via activation of NF-KappaB–inducing kinase (NIK) and IKK1, resulting in the nuclear translocation of p52-RelB heterodimers.
PMID: 18775672
Figure 1
indirect
PMID:18775672
The p100-mediated pathway, often called the noncanonical NF-KappaB pathway, is triggered by a subset of TNF family members and sequentially activates NF-KappaB inducing kinase (NIK) and IKK1.
PMID: 18775672
A limited number of agonists induce processing of p100 to p52 via activation of NF-KappaB–inducing kinase (NIK) and IKK1, resulting in the nuclear translocation of p52-RelB heterodimers.
PMID: 18775672
Figure 1
indirect
PMID:18775672
The p100-mediated pathway, often called the noncanonical NF-KappaB pathway, is triggered by a subset of TNF family members and sequentially activates NF-KappaB inducing kinase (NIK) and IKK1.
PMID: 18775672
A limited number of agonists induce processing of p100 to p52 via activation of NF-KappaB–inducing kinase (NIK) and IKK1, resulting in the nuclear translocation of p52-RelB heterodimers.
PMID: 18775672
Figure 1
indirect
PMID:18775672
The p100-mediated pathway, often called the noncanonical NF-KappaB pathway, is triggered by a subset of TNF family members and sequentially activates NF-KappaB inducing kinase (NIK) and IKK1.
PMID: 18775672
A limited number of agonists induce processing of p100 to p52 via activation of NF-KappaB–inducing kinase (NIK) and IKK1, resulting in the nuclear translocation of p52-RelB heterodimers.
indirect
PMID: 18775672,15214841
IKK1 phosphorylates p100, triggering its polyubiquitination and subsequent partial proteolysis by the proteasome to produce p52, which translocates into the nucleus predominantly in association with RelB
PMID: 18775672,11239468,16303288
IKK1 phosphorylates p100 at two C-terminal serines, which promotes p100 ubiquitination by the SCFbetaTrCP ubiquitin E3 ligase, partial proteolysis by the proteasome and subsequent nuclear translocation of p52-RelB complexes
indirect
PMID: 18775672,15214841
IKK1 phosphorylates p100, triggering its polyubiquitination and subsequent partial proteolysis by the proteasome to produce p52, which translocates into the nucleus predominantly in association with RelB
PMID: 18775672,11239468,16303288
IKK1 phosphorylates p100 at two C-terminal serines, which promotes p100 ubiquitination by the SCFbetaTrCP ubiquitin E3 ligase, partial proteolysis by the proteasome and subsequent nuclear translocation of p52-RelB complexes
PMID: 18775672,15214841
IKK1 phosphorylates p100, triggering its polyubiquitination and subsequent partial proteolysis by the proteasome to produce p52, which translocates into the nucleus predominantly in association with RelB
PMID: 18775672,11239468,16303288
IKK1 phosphorylates p100 at two C-terminal serines, which promotes p100 ubiquitination by the SCFbetaTrCP ubiquitin E3 ligase, partial proteolysis by the proteasome and subsequent nuclear translocation of p52-RelB complexes
PMID: 18775672,15214841
IKK1 phosphorylates p100, triggering its polyubiquitination and subsequent partial proteolysis by the proteasome to produce p52, which translocates into the nucleus predominantly in association with RelB
PMID: 18775672,11239468,16303288
IKK1 phosphorylates p100 at two C-terminal serines, which promotes p100 ubiquitination by the SCFbetaTrCP ubiquitin E3 ligase, partial proteolysis by the proteasome and subsequent nuclear translocation of p52-RelB complexes
indirect
PMID: 18775672
However, p105 is phosphorylated by IKK after activation of the canonical pathway, targeting it for complete degradation by the proteasome to release associated NF-KappaB subunits.
PMID: 18775672
By contrast, the canonical IKK complex triggers p105 proteolysis, which releases associated Rel subunits and also facilitates activation of the p105-associated TPL-2 MEK
kinase, which triggers extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase activation
PMID: 18775672
By contrast, the canonical IKK complex triggers p105 proteolysis, which releases associated Rel subunits and also facilitates activation of the p105-associated TPL-2 MEK
kinase, which triggers extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase activation
PMID: 18775672
However, p105 is phosphorylated by IKK after activation of the canonical pathway, targeting it for complete degradation by the proteasome to release associated NF-KappaB subunits
indirect
PMID: 18775672
However, p105 is phosphorylated by IKK after activation of the canonical pathway, targeting it for complete degradation by the proteasome to release associated NF-KappaB subunits.
PMID: 18775672
By contrast, the canonical IKK complex triggers p105 proteolysis, which releases associated Rel subunits and also facilitates activation of the p105-associated TPL-2 MEK
kinase, which triggers extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase activation
PMID: 18775672
By contrast, the canonical IKK complex triggers p105 proteolysis, which releases associated Rel subunits and also facilitates activation of the p105-associated TPL-2 MEK
kinase, which triggers extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase activation
PMID: 18775672
However, p105 is phosphorylated by IKK after activation of the canonical pathway, targeting it for complete degradation by the proteasome to release associated NF-KappaB subunits
indirect
PMID: 18775672
By contrast, the canonical IKK complex triggers p105 proteolysis, which releases associated Rel subunits and also facilitates activation of the p105-associated TPL-2 MEK
kinase, which triggers extracellular signal-regulated kinase (ERK) mitogen-activated protein (MAP) kinase activation
PMID: 18775672
Figure1
indirect
PMID: 18775672
Figure1
PMID: 18775672
In unstimulated cells, homodimers of p50 and p52 actively repress transcription of NF-κB target genes to which they are bound by recruitment of histone deacetylases (HDAC).
indirect
PMID: 18775672
Figure1
indirect
PMID: 18775672
Figure1
PMID: 18775672
In unstimulated cells, homodimers of p50 and p52 actively repress transcription of NF-κB target genes to which they are bound by recruitment of histone deacetylases (HDAC).
indirect
indirect
PMID: 18775672,15214841
Tpl-2 is a mitogen-activated protein (MAP) 3-kinase that mediates TLR-stimulated activation of extracellular signal-regulated kinase (ERK) and production of TNF-alpha in macrophages, thereby regulating inflammatory responses
PMID: 18775672
Ligation of TCR and the costimulatory molecule CD28 triggers the association of the intermediate CBM signaling complex, composed of Carma1, Bcl10 and MALT1, with the Ubc13-Uve1 ubiquitin conjugating enzyme heterodimer.
indirect
PMID: 18775672
Ligation of TCR and the costimulatory molecule CD28 triggers the association of the intermediate CBM signaling complex, composed of Carma1, Bcl10 and MALT1, with the Ubc13-Uve1 ubiquitin conjugating enzyme heterodimer
PMID: 18775672,17948050
TCR stimulation similarly promotes recruitment of TAK1 and IKK to the paracaspase MALT1, which is conjugated with K63-linked ubiquitin chains
indirect
PMID: 18775672
This mediates K63-linked ubiquitination of NEMO, Bcl10 and MALT1, promoting the interaction of the CBM complex with IKK and transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1), which is a required step for the activation of IKK.
PMID: 18775672
For example, positions K399 and K285 of NEMO are conjugated with K63-linked polyubiquitin chains in cells stimulated via the TCR (T-cell receptor) and NOD2 (nucleotide oligomerization domain), respectively.
PMID: 18775672
This mediates K63-linked ubiquitination of NEMO, Bcl10 and MALT1, promoting the interaction of the CBM complex with IKK and transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1), which is a required step for the activation of IKK.
PMID: 18775672
This mediates K63-linked ubiquitination of NEMO, Bcl10 and MALT1, promoting the interaction of the CBM complex with IKK and transforming growth factor beta (TGF-beta)-activated kinase 1 (TAK1), which is a required step for the activation of IKK.
PMID: 18775672
It is generally thought that assembly of ubiquitin-dependent signaling complexes both activates TAK1 and allows TAK1 to efficiently phosphorylate and activate IKK.
indirect
PMID: 18775672
Figure 1b
PMID: 18775672,18535581
CYLD physically interacts with and deubiquitinates NEMO, thereby negatively regulating NF-KappaB activation
PMID: 18775672,18535581
CYLD physically interacts with and deubiquitinates NEMO, thereby negatively regulating NF-KappaB activation
indirect
PMID: 18775672
On receptor ligation, TRAF2 and TRAF6 undergo self-ubiquitination and induce the ubiquitination of target proteins involved in IKK activation, such as NF-κB essential modulator (NEMO) and several signaling adaptors.
indirect
PMID: 18775672
On receptor ligation, TRAF2 and TRAF6 undergo self-ubiquitination and induce the ubiquitination of target proteins involved in IKK activation, such as NF-κB essential modulator (NEMO) and several signaling adaptors.
indirect
PMID: 18775672
On receptor ligation, TRAF2 and TRAF6 undergo self-ubiquitination and induce the ubiquitination of target proteins involved in IKK activation, such as NF-κB essential modulator (NEMO) and several signaling adaptors.
indirect
PMID: 18775672
On receptor ligation, TRAF2 and TRAF6 undergo self-ubiquitination and induce the ubiquitination of target proteins involved in IKK activation, such as NF-κB essential modulator (NEMO) and several signaling adaptors.
indirect
PMID: 18775672
On receptor ligation, TRAF2 and TRAF6 undergo self-ubiquitination and induce the ubiquitination of target proteins involved in IKK activation, such as NF-κB essential modulator (NEMO) and several signaling adaptors.
indirect
PMID: 18775672
In TNF-stimulated cells, TRAF2 mediates the K63 ubiquitination of an adaptor kinase, RIP1, which in turn recruits TAK1 and IKK complexes and mediates their catalytic activation.
PMID: 18775672
In TNF-stimulated cells, TRAF2 mediates the K63 ubiquitination of an adaptor kinase, RIP1, which in turn recruits TAK1 and IKK complexes and mediates their catalytic activation.
indirect
indirect
PMID: 18775672
For example, positions K399 and K285 of NEMO are conjugated with K63-linked polyubiquitin chains in cells stimulated via the TCR (T-cell receptor) and NOD2 (nucleotide oligomerization domain), respectively.
indirect
PMID: 18775672
By contrast, DNA damaging agents induce NEMO monoubiquitination at positions K277 and K309.
indirect
PMID: 18775672,18535581
CYLD also removes K63-linked ubiquitin from TRAF2, TRAF6, TRAF7, RIP1, TAK1 and Bcl-3
indirect
PMID: 18775672,18535581
CYLD also removes K63-linked ubiquitin from TRAF2, TRAF6, TRAF7, RIP1, TAK1 and Bcl-3
indirect
PMID: 18775672,18535581
CYLD also removes K63-linked ubiquitin from TRAF2, TRAF6, TRAF7, RIP1, TAK1 and Bcl-3
indirect
PMID: 18775672,18535581
CYLD also removes K63-linked ubiquitin from TRAF2, TRAF6, TRAF7, RIP1, TAK1 and Bcl-3
indirect
PMID: 18775672,18535581
CYLD also removes K63-linked ubiquitin from TRAF2, TRAF6, TRAF7, RIP1, TAK1 and Bcl-3
PMID: 18775672,16713561
Bcl-3 ubiquitination, by contrast, seems to promote its translocation into the nucleus, where it functions as a transcriptional coactivator of p50- and p52-containing complexes
indirect
PMID: 18775672,16713561
Bcl-3 ubiquitination, by contrast, seems to promote its translocation into the nucleus, where it functions as a transcriptional coactivator of p50- and p52-containing complexes
PMID: 18775672,15334086,18342009,14748687,15258597,16684768
Like CYLD, A20 can deubiquitinate several NF-κB regulatory proteins, including TRAF6, RIP1, RIP2 and NEMO
PMID: 18775672,15334086,18342009,14748687,15258597,16684768
Like CYLD, A20 can deubiquitinate several NF-κB regulatory proteins, including TRAF6, RIP1, RIP2 and NEMO
indirect
PMID: 18775672,15334086,18342009,14748687,15258597,16684768
Like CYLD, A20 can deubiquitinate several NF-κB regulatory proteins, including TRAF6, RIP1, RIP2 and NEMO
indirect
PMID: 18775672,15334086,18342009,14748687,15258597,16684768
Like CYLD, A20 can deubiquitinate several NF-κB regulatory proteins, including TRAF6, RIP1, RIP2 and NEMO
indirect
PMID: 18775672
A20 removes K63-linked ubiquitin chains from RIP1 and concurrently stimulates conjugation of K48-linked ubiquitin chains to RIP1, which targets it for proteasomal degradation.
PMID: 18775672
A20 removes K63-linked ubiquitin chains from RIP1 and concurrently stimulates conjugation of K48-linked ubiquitin chains to RIP1, which targets it for proteasomal degradation.
PMID: 18775672,18246070
However, it is uncertain whether the E3 ligase activity associated with A20 is intrinsic, because Itch E3 ligase can be recruited to A20 via TAX1BP1 (TAX1-binding protein 1), an adaptor that was originally found to associate with the Tax protein encoded by human T-cell leukemia virus type I
PMID: 18775672,17703191,18239685
TAX1BP1 interacts with A20 and mediates the recruitment of A20 to K63-ubiquitinated RIP1 and TRAF6
PMID: 18775672,18246070
However, it is uncertain whether the E3 ligase activity associated with A20 is intrinsic, because Itch E3 ligase can be recruited to A20 via TAX1BP1 (TAX1-binding protein 1), an adaptor that was originally found to associate with the Tax protein encoded by human T-cell leukemia virus type I
indirect
PMID: 18775672,17709380
The DUB catalytic activity of A20 might also be positively regulated through its phosphorylation by IKK2
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
PMID: 18775672
Because TRAF2 dimerizes with TRAF3 and physically interacts with c-IAPs and NIK, an attractive model is that these two TRAF members bridge NIK with its ubiquitin ligases c-IAP1 and 2, and thus both serve as essential components of the NIK-degradation complex.
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
PMID: 18775672
TNF receptor–associated factor 2 (TRAF2) and TRAF3 physically associate with cellular inhibitor of apoptosis 1 (c-IAP1; or c-IAP2) and NIK, respectively, and form a NIK-degradation complex via TRAF2-TRAF3 dimerization.
indirect
PMID: 18775672
Figure2
PMID: 18775672,15084608,18022362,16148124
For example, degradation of c-IAP1 is associated with induction of p100 processing by a TNF family member, TWEAK (TNF-like weak inducer of apoptosis) , whereas TRAF2 and TRAF3 proteolysis is induced by several other agonists of the noncanonical pathway
indirect
PMID: 18775672
Figure2
PMID: 18775672,15084608,18022362,16148124
For example, degradation of c-IAP1 is associated with induction of p100 processing by a TNF family member, TWEAK (TNF-like weak inducer of apoptosis) , whereas TRAF2 and TRAF3 proteolysis is induced by several other agonists of the noncanonical pathway
indirect
PMID: 18775672
Figure2
PMID: 18775672,15084608,18022362,16148124
For example, degradation of c-IAP1 is associated with induction of p100 processing by a TNF family member, TWEAK (TNF-like weak inducer of apoptosis) , whereas TRAF2 and TRAF3 proteolysis is induced by several other agonists of the noncanonical pathway
indirect
PMID: 18775672
Figure2
PMID: 18775672,15084608,18022362,16148124
For example, degradation of c-IAP1 is associated with induction of p100 processing by a TNF family member, TWEAK (TNF-like weak inducer of apoptosis) , whereas TRAF2 and TRAF3 proteolysis is induced by several other agonists of the noncanonical pathway
indirect
PMID: 18775672
Figure2
PMID: 18775672,15084608,18022362,16148124
For example, degradation of c-IAP1 is associated with induction of p100 processing by a TNF family member, TWEAK (TNF-like weak inducer of apoptosis) , whereas TRAF2 and TRAF3 proteolysis is induced by several other agonists of the noncanonical pathway
indirect
PMID: 18775672,17997719,18347055,18180283
However, recent evidence suggests that IRAK1 is conjugated with K63-linked ubiquitin chains and provides a binding platform for IKK and possibly other signaling complexes
PMID: 18775672,17997719,18347055,18180283
However, recent evidence suggests that IRAK1 is conjugated with K63-linked ubiquitin chains and provides a binding platform for IKK and possibly other signaling complexes
PMID: 18775672,18212736
The ABIN (A20-binding inhibitor of NF-KappaB) family proteins, ABIN-1, ABIN-2 and ABIN-3, also contain a UBD homologous to that of NEMO and can bind to K63 ubiquitinated proteins
PMID: 18775672,18212736
The ABIN (A20-binding inhibitor of NF-KappaB) family proteins, ABIN-1, ABIN-2 and ABIN-3, also contain a UBD homologous to that of NEMO and can bind to K63 ubiquitinated proteins
PMID: 18775672,18212736
The ABIN (A20-binding inhibitor of NF-KappaB) family proteins, ABIN-1, ABIN-2 and ABIN-3, also contain a UBD homologous to that of NEMO and can bind to K63 ubiquitinated proteins
PMID: 18775672,17703191,18239685
TAX1BP1 interacts with A20 and mediates the recruitment of A20 to K63-ubiquitinated RIP1 and TRAF6
PMID: 18775672,17703191,18239685
TAX1BP1 interacts with A20 and mediates the recruitment of A20 to K63-ubiquitinated RIP1 and TRAF6
indirect
PMID: 18775672,18022362,18022363
Synthetic c-IAP antagonists induce rapid degradation of c-IAP1 and c-IAP2 via the ubiquitin-proteasome pathway
PMID: 18775672,18022362,18022363
Synthetic c-IAP antagonists induce rapid degradation of c-IAP1 and c-IAP2 via the ubiquitin-proteasome pathway
indirect
PMID: 18775672,18022362,18022363
Synthetic c-IAP antagonists induce rapid degradation of c-IAP1 and c-IAP2 via the ubiquitin-proteasome pathway
PMID: 18775672,18022362,18022363
Synthetic c-IAP antagonists induce rapid degradation of c-IAP1 and c-IAP2 via the ubiquitin-proteasome pathway
PMID: 18775672
In unstimulated cells, homodimers of p50 and p52 actively repress transcription of NF-κB target genes to which they are bound by recruitment of histone deacetylases (HDAC).
PMID: 18775672
In unstimulated cells, homodimers of p50 and p52 actively repress transcription of NF-κB target genes to which they are bound by recruitment of histone deacetylases (HDAC).
indirect
PMID: 18775672
Figure 1
PMID: 18775672
In unstimulated cells, homodimers of p50 and p52 actively repress transcription of NF-κB target genes to which they are bound by recruitment of histone deacetylases (HDAC).
indirect
PMID: 18775672
S276 can be phosphorylated by protein kinase A (PKA) and mitogen- and stress-activated protein kinases (MSKs) 1 and 2, inducing binding to CREB-binding protein (CBP) and p300 co-activator complexes, which acetylate adjacent histones and RelA to stimulate target gene transcription.
PMID: 18775672
Figure 3
indirect
PMID: 18775672
S276 can be phosphorylated by protein kinase A (PKA) and mitogen- and stress-activated protein kinases (MSKs) 1 and 2, inducing binding to CREB-binding protein (CBP) and p300 co-activator complexes, which acetylate adjacent histones and RelA to stimulate target gene transcription.
PMID: 18775672
Figure 3
indirect
PMID: 18775672
S276 can be phosphorylated by protein kinase A (PKA) and mitogen- and stress-activated protein kinases (MSKs) 1 and 2, inducing binding to CREB-binding protein (CBP) and p300 co-activator complexes, which acetylate adjacent histones and RelA to stimulate target gene transcription.
PMID: 18775672
Figure 3
indirect
PMID: 18775672
IkappaB kinase 1 (IKK1)phosphorylation of CBP-p300 stimulates preferential binding to NF-KappaB complexes.
PMID: 18775672
S276 can be phosphorylated by protein kinase A (PKA) and mitogen- and stress-activated protein kinases (MSKs) 1 and 2, inducing binding to CREB-binding protein (CBP) and p300 co-activator complexes, which acetylate adjacent histones and RelA to stimulate target gene transcription
PMID: 18775672
S276 can be phosphorylated by protein kinase A (PKA) and mitogen- and stress-activated protein kinases (MSKs) 1 and 2, inducing binding to CREB-binding protein (CBP) and p300 co-activator complexes, which acetylate adjacent histones and RelA to stimulate target gene transcription
PMID: 18775672
RelA S276 phosphorylation also triggers recruitment of a complex of CDK1 and cyclin T1, which promotes transcriptional elongation.
indirect
PMID: 18775672
RelA S276 phosphorylation also triggers recruitment of a complex of CDK1 and cyclin T1, which promotes transcriptional elongation.
PMID: 18775672
Figure 3
PMID: 18775672
NF-KappaB dimers can be transported back to the cytoplasm as a result of NF-KappaB–dependent IKappaBalpha resynthesis.
PMID: 18775672
NF-KappaB dimers can be transported back to the cytoplasm as a result of NF-KappaB–dependent IKappaBalpha resynthesis.
PMID: 18775672
NF-KappaB dimers can be transported back to the cytoplasm as a result of NF-KappaB–dependent IKappaBalpha resynthesis.
PMID: 18775672
NF-KappaB dimers can be transported back to the cytoplasm as a result of NF-KappaB–dependent IKappaBalpha resynthesis.
PMID: 18775672
NF-KappaB dimers can be transported back to the cytoplasm as a result of NF-KappaB–dependent IKappaBalpha resynthesis.
indirect
indirect
PMID: 18775672
NF-KappaB dimers can be transported back to the cytoplasm as a result of NF-KappaB–dependent IKappaBalpha resynthesis.
indirect
PMID: 18775672
Alternatively, RelA can be ubiquitinated by ECSSOCS1 or PDLIM2 E3 ligases, triggering its degradation by the proteasome.
indirect
PMID: 18775672
Alternatively, RelA can be ubiquitinated by ECSSOCS1 or PDLIM2 E3 ligases, triggering its degradation by the proteasome.
PMID: 18775672
Alternatively, RelA can be ubiquitinated by ECSSOCS1 or PDLIM2 E3 ligases, triggering its degradation by the proteasome.
indirect
indirect
PMID: 18775672
c-Rel–mediated transcription is also turned off by ubiquitin-dependent proteolysis in stimulated cells
PMID: 18775672
c-Rel–mediated transcription is also turned off by ubiquitin-dependent proteolysis in stimulated cells
PMID: 18775672
c-Rel–mediated transcription is also turned off by ubiquitin-dependent proteolysis in stimulated cells
PMID: 18775672
Binding of phospho-S276-RelA is primarily restricted to a subset of genes that are rapidly induced by TNF, such as the chemokine IL-8.
PMID: 18775672
Induction of such genes involves the association of phospho-S276-RelA with the P-TEFb transcriptional elongation factor, a complex of CDK-9 (cyclin-dependent kinase-9) and cyclin T1, which controls Pol II recruitment and activation.
PMID: 18775672
Binding of phospho-S276-RelA is primarily restricted to a subset of genes that are rapidly induced by TNF, such as the chemokine IL-8.
PMID: 18775672
Induction of such genes involves the association of phospho-S276-RelA with the P-TEFb transcriptional elongation factor, a complex of CDK-9 (cyclin-dependent kinase-9) and cyclin T1, which controls Pol II recruitment and activation.
indirect
indirect
PMID: 18775672,17268554
For example, in epithelial cells, TGF-beta1 induces RelA acetylation on K221 via a Smad3 and 4–PKA–p300-dependent signaling pathway
PMID: 18775672,17268554
For example, in epithelial cells, TGF-beta1 induces RelA acetylation on K221 via a Smad3 and 4–PKA–p300-dependent signaling pathway
indirect
PMID: 18775672,17268554
For example, in epithelial cells, TGF-beta1 induces RelA acetylation on K221 via a Smad3 and 4–PKA–p300-dependent signaling pathway
PMID: 18775672,17268554
For example, in epithelial cells, TGF-beta1 induces RelA acetylation on K221 via a Smad3 and 4–PKA–p300-dependent signaling pathway
indirect
PMID: 18775672,17268554
For example, in epithelial cells, TGF-beta1 induces RelA acetylation on K221 via a Smad3 and 4–PKA–p300-dependent signaling pathway
PMID: 18775672,17268554
For example, in epithelial cells, TGF-β1 induces RelA acetylation on K221 via a Smad3 and 4–PKA–p300-dependent signaling pathway
PMID: 18775672,17183367
COMMD1 interacts with ECSSOCS1 and increases the interaction between SOCS1 and RelA
indirect
PMID: 18775672,17183367
COMMD1 interacts with ECSSOCS1 and increases the interaction between SOCS1 and RelA
indirect
PMID: 18775672,17673665
LPS stimulation of macrophages also increases the ubiquitination and proteolysis of p50 by the proteasome
PMID: 18775672
This is inhibited by BCL3, which blocks p50 ubiquitination and stabilizes a p50 complex that inhibits gene transcription.
PMID: 18775672,17673665
LPS stimulation of macrophages also increases the ubiquitination and proteolysis of p50 by the proteasome
indirect
PMID: 18775672,17540171
After TNF or LPS stimulation, PIAS1 is rapidly phosphorylated on S90, which is required for PIAS1 to block the promoter binding of RelA
indirect
PMID: 18775672,17540171
After TNF or LPS stimulation, PIAS1 is rapidly phosphorylated on S90, which is required for PIAS1 to block the promoter binding of RelA
PMID: 18775672,17540171
After TNF or LPS stimulation, PIAS1 is rapidly phosphorylated on S90, which is required for PIAS1 to block the promoter binding of RelA
indirect
PMID: 18775672,18045535
A partner of RelA, the ribosomal protein S3 (RPS3), was identified by affinity purification and shown to substantially increase the DNA binding activity of RelA-RelA homodimers and p50-RelA heterodimers.
indirect
PMID: 18775672,18045535
A partner of RelA, the ribosomal protein S3 (RPS3), was identified by affinity purification and shown to substantially increase the DNA binding activity of RelA-RelA homodimers and p50-RelA heterodimers.
PMID: 18775672
E2F1 is rapidly recruited to the promoters of these genes via its physical interaction with p50-RelA heterodimers in LPS-stimulated cells.
PMID: 18775672
RNAi knockdown revealed a requirement for E2F1 for the transcriptional activation of several LPS-inducible NF-KappaB target genes, including IL-1beta, TNF and CCL3.
PMID: 18775672
RNAi knockdown revealed a requirement for E2F1 for the transcriptional activation of several LPS-inducible NF-KappaB target genes, including IL-1beta, TNF and CCL3.
PMID: 18775672
RNAi knockdown revealed a requirement for E2F1 for the transcriptional activation of several LPS-inducible NF-KappaB target genes, including IL-1beta, TNF and CCL3.
indirect
PMID: 18775672
RNAi knockdown revealed a requirement for E2F1 for the transcriptional activation of several LPS-inducible NF-KappaB target genes, including IL-1beta, TNF and CCL3.
PMID: 18775672
E2F1 is rapidly recruited to the promoters of these genes via its physical interaction with p50-RelA heterodimers in LPS-stimulated cells.
indirect
PMID: 18775672
RNAi knockdown revealed a requirement for E2F1 for the transcriptional activation of several LPS-inducible NF-KappaB target genes, including IL-1beta, TNF and CCL3.
PMID: 18775672
E2F1 is rapidly recruited to the promoters of these genes via its physical interaction with p50-RelA heterodimers in LPS-stimulated cells.
indirect
PMID: 18775672
RNAi knockdown revealed a requirement for E2F1 for the transcriptional activation of several LPS-inducible NF-KappaB target genes, including IL-1beta, TNF and CCL3.
PMID: 18775672
E2F1 is rapidly recruited to the promoters of these genes via its physical interaction with p50-RelA heterodimers in LPS-stimulated cells.