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PMID: 18267068
IκBα is rapidly degraded during activation of canonical NF-κB signaling pathways leading to the release of multiple NF-κB dimers, although the p65:p50 heterodimer is likely the primary target of IκBα.
PMID: 18267068, 9660950
PKA exists in a complex with cytosolic NF-κB:IκB complexes and following degradation of IκBα phosphorylates p65 at Ser276, promoting the interaction of p65 with the transcriptional coactivators CBP (CREB-binding protein) and p300
PMID: 18267068, 11983155
The exposed NLS of p50 coupled with nuclear export sequences (NES) in IκBα and p65 leads to constant shuttling of IκBα/NF-κB complexes between the nucleus and the cytoplasm, despite steady-state localization that appears almost exclusively cytosolic
PMID: 18267068, 11983155
The exposed NLS of p50 coupled with nuclear export sequences (NES) in IκBα and p65 leads to constant shuttling of IκBα/NF-κB complexes between the nucleus and the cytoplasm, despite steady-state localization that appears almost exclusively cytosolic
PMID: 18267068
Constitutive binding of p50 or p52 homodimers to κB sites on NF-κB-responsive promoters may thus act to check NF-κB transactivation until displaced by transcriptionally competent NF-κB dimers.
PMID: 18267068
Constitutive binding of p50 or p52 homodimers to κB sites on NF-κB-responsive promoters may thus act to check NF-κB transactivation until displaced by transcriptionally competent NF-κB dimers.
PMID: 18267068, 16732290
Likewise it has been shown that in T cells p100 also limits p65-mediated NF-κB activity in a negative feedback loop set up following T cell activation
PMID: 18267068
Degradation of IκB is a rapidly induced signaling event that is initiated upon specific phosphorylation of these molecules by activated IKK.
PMID: 18267068
The noncanonical pathway, conversely, depends only on the IKKα subunit, which functions by phosphorylating p100 and causing its inducible processing to p52.
PMID: 18267068, 17072324
Phosphorylation of the conserved serine residues (DS*GXXS*) in IκB proteins results in their K48-linked polyubiquitination by βTrCP containing Skp1-Culin-Roc1/Rbx1/Hrt-1-F-box (SCF) E3 ubiquitin ligase complexes (SCFβTrCP) coordinately with the E2 UbcH5.
PMID: 18267068, 17072324
Phosphorylation of the conserved serine residues (DS*GXXS*) in IκB proteins results in their K48-linked polyubiquitination by βTrCP containing Skp1-Culin-Roc1/Rbx1/Hrt-1-F-box (SCF) E3 ubiquitin ligase complexes (SCFβTrCP) coordinately with the E2 UbcH5.
PMID: 18267068, 17072323
The released NF-κB dimers bind promoter and enhancer regions containing κB consensus sequences 5′ GGGRNWYYCC 3′ (N—any base; R—purine; W—adenine or thymine; and Y—pyrimidine)
PMID: 18267068, 17072323
The released NF-κB dimers bind promoter and enhancer regions containing κB consensus sequences 5′ GGGRNWYYCC 3′ (N—any base; R—purine; W—adenine or thymine; and Y—pyrimidine)
PMID: 18267068
Thus when IL-1R binds IL-1 or RIG-I binds cytoplasmic dsRNA they activate overlapping but unique signaling pathways due to these differences in upstream signaling components, and hence they induce distinct transcriptional programs.
PMID: 18267068, 17047224
For example, IL-1R and RIG-I, which both signal through TRAF6 to IKK, do so through distinct receptor proximal adaptor components MyD88 and MAVS, respectively
PMID: 18267068, 8565075
Following binding of TNFα, TRAF2 is recruited to TNFR1 through its interaction with TRADD
indirect
PMID: 18267068
It is important to bear in mind that although diverse upstream events may mediate IKK activation through a common mechanism, parallel signaling pathways emanating from nonredundant receptor proximal signaling components frequently produce crosstalk that shapes the NF-κB response in ways that are unique to individual signaling pathways.
PMID: 18267068
The core elements of NF-κB signaling pathways are generally several steps removed from the receptor itself. The intervening steps between receptor and IKK form links to parallel signaling pathways.
indirect
PMID: 18267068
It is important to bear in mind that although diverse upstream events may mediate IKK activation through a common mechanism, parallel signaling pathways emanating from nonredundant receptor proximal signaling components frequently produce crosstalk that shapes the NF-κB response in ways that are unique to individual signaling pathways.
PMID: 18267068
The core elements of NF-κB signaling pathways are generally several steps removed from the receptor itself. The intervening steps between receptor and IKK form links to parallel signaling pathways.
PMID: 18267068, 8565075
Following binding of TNFα, TRAF2 is recruited to TNFR1 through its interaction with TRADD
PMID: 18267068, 8565075
Following binding of TNFα, TRAF2 is recruited to TNFR1 through its interaction with TRADD
PMID: 18267068
TRAF5 was also shown to interact with the TNFR1 signaling complex,
indirect
PMID: 18267068
TRAF2 and TRAF5 are together required for NF-κB activation by TNFR1.
indirect
PMID: 18267068, 17047224, 17072327
In Toll/IL-1 signaling TRAF6 is recruited to the receptor complex and is necessary for MyD88-dependent activation of NF-κB by IL-1 and ligands of TLR4
PMID: 18267068, 17047224, 17072327
In Toll/IL-1 signaling TRAF6 is recruited to the receptor complex and is necessary for MyD88-dependent activation of NF-κB by IL-1 and ligands of TLR4
PMID: 18267068, 17047224, 17072327
In Toll/IL-1 signaling TRAF6 is recruited to the receptor complex and is necessary for MyD88-dependent activation of NF-κB by IL-1 and ligands of TLR4
PMID: 18267068, 17047224, 17072327
In Toll/IL-1 signaling TRAF6 is recruited to the receptor complex and is necessary for MyD88-dependent activation of NF-κB by IL-1 and ligands of TLR4
PMID: 18267068, 15708970
TRAF3, which interacts with receptors that trigger the alternative pathway, also interacts with NIK and it now appears that theactivation of NIK is negatively regulated by TRAF3.
PMID: 18267068, 15708970
TRAF3, which interacts with receptors that trigger the alternative pathway, also interacts with NIK and it now appears that the activation of NIK is negatively regulated by TRAF3.
PMID: 18267068, 15084608
In the resting state, TRAF3 induces NIK ubiquitination and degradation, but upon stimulation TRAF3 undergoes signal-dependent degradation, mediated by other TRAF family members, resulting in the accumulation and activation of NIK and consequent activation of the noncanonical pathway
PMID: 18267068, 15084608
In the resting state, TRAF3 induces NIK ubiquitination and degradation, but upon stimulation TRAF3 undergoes signal-dependent degradation, mediated by other TRAF family members, resulting in the accumulation and activation of NIK and consequent activation of the noncanonical pathway
PMID: 18267068, 15084608
In the resting state, TRAF3 induces NIK ubiquitination and degradation, but upon stimulation TRAF3 undergoes signal-dependent degradation, mediated by other TRAF family members, resulting in the accumulation and activation of NIK and consequent activation of the noncanonical pathway
PMID: 18267068, 15084608
In the resting state, TRAF3 induces NIK ubiquitination and degradation, but upon stimulation TRAF3 undergoes signal-dependent degradation, mediated by other TRAF family members, resulting in the accumulation and activation of NIK and consequent activation of the noncanonical pathway
PMID: 18267068
RIP family members have been implicated in most TRAF-dependent pathways, e.g., signaling from TNFR superfamily and Toll/IL-1R.
PMID: 18267068
RIP1 binds to NEMO and is essential for TNFα-induced IKK and NF-κB activation
PMID: 18267068, 8565075, 9529147, 8947041, 10755617
RIP1 binds to NEMO and is essential for TNFα-induced IKK and NF-κB activation
PMID: 18267068
Thus when IL-1R binds IL-1 or RIG-I binds cytoplasmic dsRNA they activate overlapping but unique signaling pathways due to these differences in upstream signaling components, and hence they induce distinct transcriptional programs.
PMID: 18267068, 17047224
For example, IL-1R and RIG-I, which both signal through TRAF6 to IKK, do so through distinct receptor proximal adaptor components MyD88 and MAVS, respectively
PMID: 18267068, 8565075, 9529147, 8947041, 10755617
RIP1 binds to NEMO and is essential for TNFα-induced IKK and NF-κB activation
PMID: 18267068, 11359906
In the absence of RIP1, IKK recruitment occurs through TRAF2 but does not lead to IKK activation
PMID: 18267068, 16603398, 16543241
RIP1 is inducibly ubiquitinated by TRAF2 following TNFα stimulation.
PMID: 18267068, 16547522
RIP also becomes rapidly ubiquitinated following TNFα stimulation, and it has been proposed that it is through this posttranslational modification that RIP1 binds to NEMO.
PMID: 18267068, 15064760, 16115877
In addition to TNFR1 signaling, and IKK activation via other death domain-containing TNFR family members, RIP1 has also been reported to be required for TRIF-dependent NF-κB activation via TLR3 and TLR4, as well as for NF-κB activation via RIG-I
PMID: 18267068, 15064760, 16115877
In addition to TNFR1 signaling, and IKK activation via other death domain-containing TNFR family members, RIP1 has also been reported to be required for TRIF-dependent NF-κB activation via TLR3 and TLR4, as well as for NF-κB activation via RIG-I
PMID: 18267068, 15064760, 16115877
In addition to TNFR1 signaling, and IKK activation via other death domain-containing TNFR family members, RIP1 has also been reported to be required for TRIF-dependent NF-κB activation via TLR3 and TLR4, as well as for NF-κB activation via RIG-I
PMID: 18267068, 15064760, 16115877
In addition to TNFR1 signaling, and IKK activation via other death domain-containing TNFR family members, RIP1 has also been reported to be required for TRIF-dependent NF-κB activation via TLR3 and TLR4, as well as for NF-κB activation via RIG-I
PMID: 18267068, 15064760, 16115877
In addition to TNFR1 signaling, and IKK activation via other death domain-containing TNFR family members, RIP1 has also been reported to be required for TRIF-dependent NF-κB activation via TLR3 and TLR4, as well as for NF-κB activation via RIG-I
indirect
PMID: 18267068, 15064760, 16115877
In addition to TNFR1 signaling, and IKK activation via other death domain-containing TNFR family members, RIP1 has also been reported to be required for TRIF-dependent NF-κB activation via TLR3 and TLR4, as well as for NF-κB activation via RIG-I
indirect
PMID: 18267068, 15064760, 16115877
In addition to TNFR1 signaling, and IKK activation via other death domain-containing TNFR family members, RIP1 has also been reported to be required for TRIF-dependent NF-κB activation via TLR3 and TLR4, as well as for NF-κB activation via RIG-I
indirect
PMID: 18267068
Both BCL10 and CARD11 (CARMA1) are CARD-containing proteins that are crucial for IKK activation downstream of either the T cell or B cell antigen receptors.
PMID: 18267068, 17098202
The most notable feature of the BCL10, CARD11, MALT1 (CBM) complex is its induced oligomerization following signaling, which is thought to be a key event in IKK activation downstream of these CARD-containing adaptor proteins
PMID: 18267068
Members of the NOD-LRR family of intracellular pattern recognition receptors are CARD-containing proteins that can activate IKKβ via RIP2.
PMID: 18267068, 10880512
RIP2 binds to NEMO and is believed to directly mediate activation of the IKK complex by proximity-induced mechanisms
PMID: 18267068, 17047224
NIK directly phosphorylates and activates IKKα.
PMID: 18267068, 17047224, 17072322
The alternative pathway relies on the activation of IKKα by the NF-κB-inducing kinase (NIK).
PMID: 18267068
Active IKKβ is phosphorylated on two serines, Ser177 and Ser181, within the activation loop of the kinase domain, and IKKα is similarly phosphorylated on activation loop serine residues 176 and 180.
PMID: 18267068, 17996648, 18022362, 18022363
In addition to TRAF3, cIAP1 and cIAP2 have been implicated as E3 ligases responsible for regulating constitutive NIK levels
PMID: 18267068, 17996648, 18022362, 18022363
In addition to TRAF3, cIAP1 and cIAP2 have been implicated as E3 ligases responsible for regulating constitutive NIK levels
PMID: 18267068, 10823818
It appears that IKKα and IKKβ preferentially form heterodimers in vivo, and in vitro studies indicate that IKKα/IKKβ heterodimers have higher catalytic efficiency than either homodimer
PMID: 18267068, 9346484, 9346485, 9346241
IKKα and IKKβ dimerize through the leucine zipper domain, which is also required for kinase activity.
PMID: 18267068, 9346484, 9346485, 9346241
IKKα and IKKβ dimerize through the leucine zipper domain, which is also required for kinase activity.
PMID: 18267068, 12244103, 10968790
IKKα and IKKβ bind NEMO through the C-terminal hexapeptide NEMO-binding domain (NBD) (Leu-Asp-Trp-Ser-Trp-Leu)
PMID: 18267068, 12244103
Competition experiments and biophysical analyses using the NBD peptide indicate that IKKβ binds to NEMO with considerably higher affinity than IKKα
PMID: 18267068, 12244103, 10968790
IKKα and IKKβ bind NEMO through the C-terminal hexapeptide NEMO-binding domain (NBD) (Leu-Asp-Trp-Ser-Trp-Leu)
PMID: 18267068, 12244103
Competition experiments and biophysical analyses using the NBD peptide indicate that IKKβ binds to NEMO with considerably higher affinity than IKKα
PMID: 18267068
Multiple lines of evidence point toward an IKK kinase complex that is composed of only IKKα, IKKβ, and NEMO.
PMID: 18267068, 17924664
Recombinant NEMO and IKKβ appear to associate in a 2:2 molar ratio and the minimum interaction domains form a dimer of dimers (tetramer) that can further assemble into octamers and dodecamers
PMID: 18267068
The first is the kinase chaperone HSP-90/Cdc37 that has been reported to constitutively associate with the IKK complex.
indirect
PMID: 18267068, 11864612
The HSP-90 inhibitor geldanamycin has also been shown to inhibit activation of IKK by TNF-α
PMID: 18267068, 15218148
The second interacting protein that requires mentioning is ELKS, which has been proposed to be a regulatory component of the IKK complex in addition to NEMO
PMID: 18267068
Active IKKβ is phosphorylated on two serines, Ser177 and Ser181, within the activation loop of the kinase domain, and IKKα is similarly phosphorylated on activation loop serine residues 176 and 180.
indirect
indirect
PMID: 18267068
Both BCL10 and CARD11 (CARMA1) are CARD-containing proteins that are crucial for IKK activation downstream of either the T cell or B cell antigen receptors.
PMID: 18267068, 17098202
The most notable feature of the BCL10, CARD11, MALT1 (CBM) complex is its induced oligomerization following signaling, which is thought to be a key event in IKK activation downstream of these CARD-containing adaptor proteins
PMID: 18267068, 17098202
In AgR signaling the CBM complex also assembles into a higher-order oligomer following signaling.
PMID: 18267068, 15107419, 12612076, 17924664
NEMO can form tetramers in vitro and also is reported to oligomerize in vivo, although the stoichiometry of endogenous NEMO is debatable
PMID: 18267068
both IKKα and IKKβ phosphorylate IκBα at Ser32 and Ser36 and IκBβ at Ser19 and Ser23
PMID: 18267068, 9721103
IκBα bound to NF-κB is thought to be a preferred substrate to free IκBα
PMID: 18267068
both IKKα and IKKβ prefer IκBα to IκBβ, which is consistent with the difference in IκBα and β degradation
PMID: 18267068
both IKKα and IKKβ phosphorylate IκBα at Ser32 and Ser36 and IκBβ at Ser19 and Ser23
PMID: 18267068, 9721103
IκBα bound to NF-κB is thought to be a preferred substrate to free IκBα
PMID: 18267068
both IKKα and IKKβ prefer IκBα to IκBβ, which is consistent with the difference in IκBα and β degradation
PMID: 18267068
both IKKα and IKKβ phosphorylate IκBα at Ser32 and Ser36 and IκBβ at Ser19 and Ser23
PMID: 18267068
both IKKα and IKKβ prefer IκBα to IκBβ, which is consistent with the difference in IκBα and β degradation
PMID: 18267068
both IKKα and IKKβ phosphorylate IκBα at Ser32 and Ser36 and IκBβ at Ser19 and Ser23
PMID: 18267068
both IKKα and IKKβ prefer IκBα to IκBβ, which is consistent with the difference in IκBα and β degradation
PMID: 18267068
The nuclear NF-κB drives IκBα expression generating a negative feedback loop.
PMID: 18267068
Like IκBα, IκBvar epsilon is degraded in an IKK-dependent manner and its expression is upregulated by NF-κB.
PMID: 18267068, 8816457, 7867065
IκBβ is capable of associating with NF-κB dimers that are bound to DNA.
PMID: 18267068, 17072324, 15371334
Multiple reports have demonstrated that IKKβ-dependent phosphorylation of the C-terminal region of p105 at Ser923 and Ser927 (Ser933 in human p105) leads to complete degradation of the protein analogous to IκBα
PMID: 18267068, 16619030
Normal processing of p105 to p50 in an E1 Ub-activating enzyme-deficient cell line, complemented by in vitro analysis, strongly suggests that p105 processing can occur via the 20S proteasome, independent of ubiquitination, and in a manner that is inconsistent with cotranslational processing
PMID: 18267068
Thus unprocessed p105 acts as an IκB protein that binds NF-κB dimers and can be inducibly degraded upon IKK activation.
PMID: 18267068
Thus unprocessed p105 acts as an IκB protein that binds NF-κB dimers and can be inducibly degraded upon IKK activation.
PMID: 18267068, 11687592
Regulation of RelB by p100 is especially crucial because RelB-containing dimers only associate with p100, and it has been suggested that they require p100 binding for stabilization
PMID: 18267068, 16303288, 12185077, 14676825
Phosphorylation of p100 at serines 866, 870, and 872 (Ser865, 869, and 871 in human p100) leads to the recruitment of SCFβTrCP, polyubiquitination of Lys855 in a region with sequence homology to Lys22 of IκBα, and subsequent degradation or processing to p52
PMID: 18267068, 16303288, 12185077, 14676825
Phosphorylation of p100 at serines 866, 870, and 872 (Ser865, 869, and 871 in human p100) leads to the recruitment of SCFβTrCP, polyubiquitination of Lys855 in a region with sequence homology to Lys22 of IκBα, and subsequent degradation or processing to p52
PMID: 18267068
The noncanonical or alternative NF-κB pathway, however, proceeds through proteasomal processing, rather than degradation, of p100 to p52, thereby liberating p52 containing NF-κB dimers that drive a transcriptional response that is distinct from that induced by the canonical, IκBα-regulated pathway.
PMID: 18267068, 16303288, 12185077, 14676825
Phosphorylation of p100 at serines 866, 870, and 872 (Ser865, 869, and 871 in human p100) leads to the recruitment of SCFβTrCP, polyubiquitination of Lys855 in a region with sequence homology to Lys22 of IκBα, and subsequent degradation or processing to p52
PMID: 18267068, 17254973
In addition to IκBα/β/var epsilon, p100 can also act as a traditional IκB regulating p65-containing complexes downstream of IKKα
PMID: 18267068, 17072328, 16470223
Because p100 undergoes constitutive processing in certain tissues, RelB/p52 heterodimers may exhibit constitutive activation and RelB-deficient mice have decreased baseline NF-κB activity in the thymus and spleen
PMID: 18267068
Bcl-3 is found in the nucleus associated with p50- and p52-containing homo- and heterodimers.
PMID: 18267068
Bcl-3 is found in the nucleus associated with p50- and p52-containing homo- and heterodimers.
PMID: 18267068
Bcl-3 is found in the nucleus associated with p50- and p52-containing homo- and heterodimers.
PMID: 18267068, 17673665
Bcl-3 may also stabilize repressive p50 homodimers and inhibit NF-κB activation by preventing the access of TAD-containing dimers to κB sites
PMID: 18267068, 12808109, 11713278
Cyclin D1 is a Bcl-3-regulated gene that is of particular interest owing to its role in cell proliferation and cancer.
PMID: 18267068, 16384933
Bcl-3 has also recently been implicated in the regulation of p53 by enhancing the transcription of Hdm2 in normal and cancer cells
indirect
PMID: 18267068, 15371334
IκBζ is not expressed constitutively but rather is upregulated in response to IL-1 and TLR4 ligands, but not TNF, and upon expression localizes to the nucleus
indirect
PMID: 18267068, 15371334
IκBζ is not expressed constitutively but rather is upregulated in response to IL-1 and TLR4 ligands, but not TNF, and upon expression localizes to the nucleus
indirect
PMID: 18267068, 15371334
IκBζ is not expressed constitutively but rather is upregulated in response to IL-1 and TLR4 ligands, but not TNF, and upon expression localizes to the nucleus
indirect
PMID: 18267068, 15371334
IκBζ is not expressed constitutively but rather is upregulated in response to IL-1 and TLR4 ligands, but not TNF, and upon expression localizes to the nucleus
PMID: 18267068, 15371334
IκBζ is not expressed constitutively but rather is upregulated in response to IL-1 and TLR4 ligands, but not TNF, and upon expression localizes to the nucleus
PMID: 18267068
IκBζ is inducibly expressed following NF-κB activation and once expressed associates primarily with p50 homodimers.
PMID: 18267068, 15241416
IκBζ is found associated with p50 on the promoter of IL-6, which is not inducibly expressed in IκBζ knockout cells, and it is, therefore, hypothesized that IκBζ acts as a coactivator for p50 homodimers
PMID: 18267068, 9660950
PKA exists in a complex with cytosolic NF-κB:IκB complexes and following degradation of IκBα phosphorylates p65 at Ser276, promoting the interaction of p65 with the transcriptional coactivators CBP (CREB-binding protein) and p300
PMID: 18267068
In addition to PKA, other kinases, most notably MSK1 and MSK2 (mitogen- and stress-activated protein kinase), have been reported to phosphorylate Ser276 of p65.
PMID: 18267068
In addition to PKA, other kinases, most notably MSK1 and MSK2 (mitogen- and stress-activated protein kinase), have been reported to phosphorylate Ser276 of p65.
PMID: 18267068, 15122352, 17072324
IKKα and IKKβ have been implicated in the direct phosphorylation of p65 at Ser536
PMID: 18267068, 15122352, 17072324
IKKα and IKKβ have been implicated in the direct phosphorylation of p65 at Ser536
PMID: 18267068, 9405476, 10938077
Ser529 of p65 may also be inducibly phosphorylated by CK2 following IL-1 or TNF-α stimulation, although it is unclear whether Ser529 phosphorylation affects transcription
PMID: 18267068, 12881425
PKCζ can phosphorylate p65 at Ser311, and CBP fails to associate with p65 following stimulation of PKCζ-deficient cells
PMID: 18267068, 9660950
PKA exists in a complex with cytosolic NF-κB:IκB complexes and following degradation of IκBα phosphorylates p65 at Ser276, promoting the interaction of p65 with the transcriptional coactivators CBP (CREB-binding protein) and p300.
PMID: 18267068, 17434128
It was recently reported that IKKα phosphorylates CBP in a stimulus-dependent manner, inducing upregulation of CBP activity, increased binding to p65, and decreased binding to p53
PMID: 18267068, 15122352
Acetylation of p65, probably by CBP/p300 and associated HATs, occurs in the nucleus and is associated with increased transcription
PMID: 18267068
p65 phosphorylation is necessary to recruit CBP/p300 allowing acetylation at Lys310
PMID: 18267068, 16382138
One possibility is that Ser536 phosphorylation alters the interaction of p65 with the SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) corepressor complex such that the level of HDAC3 is decreased and CBP/p300 is increased.
PMID: 18267068, 16382138
In addition to p65 phosphorylation, IKKα also may promote Lys310 acetylation through direct phosphorylation of SMRT, which leads to displacement of HDAC3 from the SMRT corepressor complex.
PMID: 18267068, 12789343, 12789342
IKKα is found associated with the κB sites of some NF-κB-responsive genes, and stimulus-induced phosphorylation of histone H3 on serine 10 does not occur in the absence of IKKα
PMID: 18267068, 17434128
In addition to the SMRT and N-CoR (nuclear receptor corepressor) complexes, IKKα also has been shown to phosphorylate the CBP coactivator
PMID: 18267068, 16382138
In addition to p65 phosphorylation, IKKα also may promote Lys310 acetylation through direct phosphorylation of SMRT, which leads to displacement of HDAC3 from the SMRT corepressor complex.
PMID: 18267068
Figure.4
PMID: 18267068, 17434128
It was recently reported that IKKα phosphorylates CBP in a stimulus-dependent manner, inducing upregulation of CBP activity, increased binding to p65, and decreased binding to p53
PMID: 18267068, 16007092
GSK3β, normally constitutively active, phosphorylates and inactivates CREB disrupting the interaction between CREB and CBP
PMID: 18267068, 16007092
GSK3β, normally constitutively active, phosphorylates and inactivates CREB disrupting the interaction between CREB and CBP
PMID: 18267068
One potential explanation is that CBP bound to CREB is a poor substrate for IKKα phosphorylation, and that CBP phosphorylated by IKKα binds poorly to CREB.
PMID: 18267068, 18045535
One recent and intriguing addition to this list is ribosomal protein S3 (RPS3), which seems to be required for the binding of NF-κB at specific κB sites
PMID: 18267068, 17377533
IKKα represses transcription of the tumor suppressor Maspin by acting at the maspin promoter strongly supports a direct mechanism of action by IKKα that is independent of NF-κB
PMID: 18267068, 17183367
Although the exact mechanism of action remains unclear, it has recently been shown that targeting the SOCS-1-containing ubiquitin ligase complex (ECSSOCS1) to p65-containing dimers is carried out by COMMD1 (Copper Metabolism MURR1 Domain containing-1) proteins
indirect
PMID: 18267068, 15858576, 16116086
IKKα is also involved in termination of inflammatory transcriptional responses in macrophages, possibly by promoting the nuclear degradation of both p65 and c-Rel
indirect
PMID: 18267068, 15858576, 16116086
IKKα is also involved in termination of inflammatory transcriptional responses in macrophages, possibly by promoting the nuclear degradation of both p65 and c-Rel
PMID: 18267068, 16547522
RIP also becomes rapidly ubiquitinated following TNFα stimulation, and it has been proposed that it is through this posttranslational modification that RIP1 binds to NEMO.
PMID: 18267068
Conformational changes in the IKK complex induced by binding of NEMO to RIP, and/or ubiquitination of NEMO, lead to the exposure of IKK kinase domain and T loop serines and consequent transautophosphorylation or phosphorylation by an IKK-K such as TAK1.
PMID: 18267068
Conformational changes in the IKK complex induced by binding of NEMO to RIP, and/or ubiquitination of NEMO, lead to the exposure of IKK kinase domain and T loop serines and consequent transautophosphorylation or phosphorylation by an IKK-K such as TAK1.
PMID: 18267068
The active IKK then phosphorylates downstream substrates, including serine 740 within the IKK NBD and serine 68 in NEMO.
PMID: 18267068
NEMO phosphorylation results in the separation of stable NEMO dimers and NEMO binding to IKK.
PMID: 18267068, 16126728, 17188031
the protein phosphatase 2A (PP2A) has been shown to associate with IKK and potentiate IKK activation in cells
PMID: 18267068, 16126728, 14585847, 17977820
structural changes induced by NEMO Ser68 and IKK NBD phosphorylation may allow dephosphorylation of the activation loop serines in IKKs as well as N-terminal phosphorylation sites in NEMO by PP2A or PP2Cβ
PMID: 18267068, 17947236, 18079694, 17277144
Similar to RIP1, the kinase activity of RIP2 does not appear to be required, and RIP2 is also ubiquitinated through the action of Ubc13/TRAF6
indirect
indirect
PMID: 18267068, 17562858, 17965022
RIP2 acts with TAK1 and TRAFs to induce NEMO ubiquitination and downstream signaling pathways