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PMID: 12213596, 10837071
Phosphorylation triggers a signal that induces ubiquitin-dependent, proteasome-mediated degradation of IkappaB-alpha, and subsequent nuclear translocation of the NF-kappaB dimers.
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PMID: 12213596
Once produced, these secreted proteins act in a paracrine fashion to induce gene expression in target cells in the adjacent microenvironment, through engagement of cell surface IFN receptors and the JAK-STAT signaling pathway.
PMID: 12213596, 11585785, 11544356
STAT1/2 heterodimers, in conjunction with interferon-stimulated gene factor 3gamma (ISGF3gamma/IRF-9) bind to ISRE found in numerous IFN-induced genes, such as 2′–5′ oligoadenylate synthase and the dsRNA activated kinase (PKR), resulting in the induction of proteins which impair viral gene expression and replication [2 and 3].
PMID: 12213596, 11585785, 11544356
STAT1/2 heterodimers, in conjunction with interferon-stimulated gene factor 3gamma (ISGF3gamma/IRF-9) bind to ISRE found in numerous IFN-induced genes, such as 2′–5′ oligoadenylate synthase and the dsRNA activated kinase (PKR), resulting in the induction of proteins which impair viral gene expression and replication [2 and 3].
PMID: 12213596, 11585785, 11544356
STAT1/2 heterodimers, in conjunction with interferon-stimulated gene factor 3gamma (ISGF3gamma/IRF-9) bind to ISRE found in numerous IFN-induced genes, such as 2′–5′ oligoadenylate synthase and the dsRNA activated kinase (PKR), resulting in the induction of proteins which impair viral gene expression and replication [2 and 3].
PMID: 12213596, 11585785, 11544356
STAT1/2 heterodimers, in conjunction with interferon-stimulated gene factor 3gamma (ISGF3gamma/IRF-9) bind to ISRE found in numerous IFN-induced genes, such as 2′–5′ oligoadenylate synthase and the dsRNA activated kinase (PKR), resulting in the induction of proteins which impair viral gene expression and replication [2 and 3].
Indirect
PMID: 12213596, 11585785, 11544356
STAT1/2 heterodimers, in conjunction with interferon-stimulated gene factor 3gamma (ISGF3gamma/IRF-9) bind to ISRE found in numerous IFN-induced genes, such as 2′–5′ oligoadenylate synthase and the dsRNA activated kinase (PKR), resulting in the induction of proteins which impair viral gene expression and replication [2 and 3].
PMID: 12213596, 11585785
The intracellular target of dsRNA is PKR, a Ser/Thr kinase that is induced by IFNs and activated catalytically through the binding of dsRNA.
Indirect
PMID: 12213596, 11585785, 11544356
STAT1/2 heterodimers, in conjunction with interferon-stimulated gene factor 3gamma (ISGF3gamma/IRF-9) bind to ISRE found in numerous IFN-induced genes, such as 2′–5′ oligoadenylate synthase and the dsRNA activated kinase (PKR), resulting in the induction of proteins which impair viral gene expression and replication [2 and 3].
PMID: 12213596, 11191641
TLR4 is essential for the recognition of LPS, the major component of the outer membrane of Gram-negative bacteria.
PMID: 12213596, 11062499
The innate immune response to RSV is mediated by the interaction of fusion protein of RSV with TLR4 and CD-14.
PMID: 12213596, 11554921
TLR2 in conjunction with TLR6, and possibly other TLRs, is essential for the recognition of lipoproteins and peptidoglycan molecules found on pathogens such as Gram-negative bacteria, Gram-positive bacteria, mycobacteria, spirochetes, and zymozan from fungi.
PMID: 12213596, 11554921
TLR2 in conjunction with TLR6, and possibly other TLRs, is essential for the recognition of lipoproteins and peptidoglycan molecules found on pathogens such as Gram-negative bacteria, Gram-positive bacteria, mycobacteria, spirochetes, and zymozan from fungi.
PMID: 12213596, 11554921
TLR2 in conjunction with TLR6, and possibly other TLRs, is essential for the recognition of lipoproteins and peptidoglycan molecules found on pathogens such as Gram-negative bacteria, Gram-positive bacteria, mycobacteria, spirochetes, and zymozan from fungi.
PMID: 12213596, 11607032
TLR3 is associated with the binding and activation of dsRNA signaling.
PMID: 12213596, 11554921
TLR5 is responsible for the recognition of flagellin, a monomeric constituent of bacterial flagella.
PMID: 12213596, 11554921, 11470918
TLR9 is essential for the recognition of bacterial CpG DNA, a motif found in non-methylated bacterial DNA.
PMID: 12213596
Activated TLRs associate with a cytoplasmic adapter molecule, MyD88, through the homophilic interaction between their TIR domains.
PMID: 12213596
Activated TLRs associate with a cytoplasmic adapter molecule, MyD88, through the homophilic interaction between their TIR domains.
PMID: 12213596
MyD88 interacts with the Ser/Thr kinase IRAK which subsequently activates the TRAF6 adapter.
PMID: 12213596
MyD88 interacts with the Ser/Thr kinase IRAK which subsequently activates the TRAF6 adapter.
PMID: 12213596
MyD88 interacts with the Ser/Thr kinase IRAK which subsequently activates the TRAF6 adapter.
Indirect
PMID: 12213596
TRAF6 in turn activates the stress-related MAPK pathways JNK and p38, as well as the IKK complex leading to AP-1 and NF-kappaB activation respectively, and the induction of cytokines such as TNF-alpha and IL-6.
PMID: 11213596
The rate limiting step in this process is the activation of the IKK complex, which is composed of two catalytic subunits—IKKalpha and IKKbeta and one regulatory subunit IKKgamma.
Indirect
PMID: 12213596
Virus infection results in the activation of multiple signaling cascades resulting in the phosphorylation of ATF-2, C-Jun, IRF-3, and NF-kapppaB.
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596
The heterodimers ATF-2/c-Jun are expressed as nuclear proteins that are activated by phosphorylation of their activation domains by p38/JNK.
Indirect
PMID: 1213596
The NF-kappaB factors are retained in the cytoplasm of non-stimulated cells in association with inhibitory subunits—inhibitors kappa B (IκBs); dsRNA- and virus-induced phosphorylation at conserved N-terminal residues (Ser 32 and 36) of IkappaB-alpha is accomplished by the IκB kinase (IKK) complex.
PMID: 12213596, 10837071
Phosphorylation triggers a signal that induces ubiquitin-dependent, proteasome-mediated degradation of IkappaB-alpha, and subsequent nuclear translocation of the NF-kappaB dimers.
PMID: 12213596, 10626894, 10848580
Another putative target of PKR is the IKKbeta subunit of the IKK complex that physically associates with PKR [20] and is believed to mediate the NF-kappaB activation in a manner that is independent of PKR kinase activity.
PMID: 12213596, 11607032
Activation of TLR-3 induces the activation of both MAPK and NF-kappaB pathways, independently of the adapter protein MyD88.
PMID: 12213596
These experiments imply that MEKK1 can induce IRF-3 and ATF2/c-Jun through the JNK pathway and NF-kappaB through the IKK pathway, resulting in the integration of multiple signal transduction pathways leading to the proper assembly of the IFN-beta enhanceosome.
PMID: 12213596, 10837071
Phosphorylation triggers a signal that induces ubiquitin-dependent, proteasome-mediated degradation of IkappaB-alpha, and subsequent nuclear translocation of the NF-kappaB dimers.
PMID: 12213596, 10626894, 10848580
Another putative target of PKR is the IKKbeta subunit of the IKK complex that physically associates with PKR [20] and is believed to mediate the NF-kappaB activation in a manner that is independent of PKR kinase activity.
PMID: 12213596, 11607032
Activation of TLR-3 induces the activation of both MAPK and NF-kappaB pathways, independently of the adapter protein MyD88.
PMID: 12213596
These experiments imply that MEKK1 can induce IRF-3 and ATF2/c-Jun through the JNK pathway and NF-kappaB through the IKK pathway, resulting in the integration of multiple signal transduction pathways leading to the proper assembly of the IFN-beta enhanceosome.
PMID: 12213596, 10837071
Phosphorylation triggers a signal that induces ubiquitin-dependent, proteasome-mediated degradation of IkappaB-alpha, and subsequent nuclear translocation of the NF-kappaB dimers.
Indirect
PMID: 12213596
TRAF6 in turn activates the stress-related MAPK pathways JNK and p38, as well as the IKK complex leading to AP-1 and NF-kappaB activation respectively, and the induction of cytokines such as TNF-alpha and IL-6.
Indirect
PMID: 12213596
TRAF6 in turn activates the stress-related MAPK pathways JNK and p38, as well as the IKK complex leading to AP-1 and NF-kappaB activation respectively, and the induction of cytokines such as TNF-alpha and IL-6.
PMID: 12213596, 10837071
Phosphorylation triggers a signal that induces ubiquitin-dependent, proteasome-mediated degradation of IkappaB-alpha, and subsequent nuclear translocation of the NF-kappaB dimers.
PMID: 12213596, 10626894, 10848580
Another putative target of PKR is the IKKbeta subunit of the IKK complex that physically associates with PKR [20] and is believed to mediate the NF-kappaB activation in a manner that is independent of PKR kinase activity.
PMID: 12213596, 11607032
Activation of TLR-3 induces the activation of both MAPK and NF-kappaB pathways, independently of the adapter protein MyD88.
PMID: 12213596
These experiments imply that MEKK1 can induce IRF-3 and ATF2/c-Jun through the JNK pathway and NF-kappaB through the IKK pathway, resulting in the integration of multiple signal transduction pathways leading to the proper assembly of the IFN-beta enhanceosome.
Indirect
Indirect
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596
The heterodimers ATF-2/c-Jun are expressed as nuclear proteins that are activated by phosphorylation of their activation domains by p38/JNK.
PMID: 12213596
TRAF6 in turn activates the stress-related MAPK pathways JNK and p38, as well as the IKK complex leading to AP-1 and NF-kappaB activation respectively, and the induction of cytokines such as TNF-alpha and IL-6.
PMID: 12213596
TRAF6 in turn activates the stress-related MAPK pathways JNK and p38, as well as the IKK complex leading to AP-1 and NF-kappaB activation respectively, and the induction of cytokines such as TNF-alpha and IL-6.
PMID: 12213596
The dsRNA mimetic poly(I:C) has the capacity to induce a subset of ISGs and cytokines that function to impede viral replication.
Indirect
PMID: 12213596
The dsRNA mimetic poly(I:C) has the capacity to induce a subset of ISGs and cytokines that function to impede viral replication.
Indirect
PMID: 12213596
The dsRNA mimetic poly(I:C) has the capacity to induce a subset of ISGs and cytokines that function to impede viral replication.
Indirect
PMID: 12213596, 11401490
Indeed, PACT, a dsRNA-binding protein originally identified as an activator of PKR, was shown to enhance IRF-3 activation.
Indirect
PMID: 12213596
Viral nucleocapsid (N) and dsRNA activate VAK, a virus activated kinase, leading to C-terminal phosphorylation of IRF-3.
PMID: 12213596
Virus-mediated activation of IRF-3 through VAK is dependent on viral entry and transcription, since replication deficient virus failed to induce IRF-3 activity.
PMID: 12213596, 11907205
Indeed, a recent study has shown that the N nucleocapsid (N) protein of MeV induced IRF-3 activation via the induction of VAK.
PMID: 12213596
IRF-3 C-terminal phosphorylation results in homodimerization, accumulation in the nucleus through CBP association, activation of genes through DNA binding and degradation by the proteasome pathway.
PMID: 12213596, 9566918, 9463386, 10082512
In addition, IRF-3 C-terminal phosphorylation is required for association with the histone acetyltransferase nuclear proteins CBP and p300 [10, 13 and 23] causing IRF-3, which normally shuttles into and out of the nucleus, to become predominantly nuclear.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
PMID: 12213596, 9566918, 9463386, 10082512
In addition, IRF-3 C-terminal phosphorylation is required for association with the histone acetyltransferase nuclear proteins CBP and p300 [10, 13 and 23] causing IRF-3, which normally shuttles into and out of the nucleus, to become predominantly nuclear.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
PMID: 12213596, 9566918, 9660935, 9463386
The activated form of IRF-3, bound to CBP, induces transcription through distinct positive regulatory domains in the type 1 IFN promoters, and through select ISRE sites.
Indirect
PMID: 12213596
Genes targeted by IRF-3 include not only the classical IRF-responsive genes IFNalpha1 and beta but also new candidates such as genes encoding for the chemokine RANTES and the cytokine IL-15.
Indirect
PMID: 12213596
Genes targeted by IRF-3 include not only the classical IRF-responsive genes IFNalpha1 and beta but also new candidates such as genes encoding for the chemokine RANTES and the cytokine IL-15.
PMID: 12213596, 10678979, 11896392
Treatment of murine macrophages with LPS also induces the production of IFNbeta, suggesting the activation of some IRF members by LPS [4 and 5] and also implying a role for ISGs in response to bacterial infection.
Indirect
PMID: 12213596
Genes targeted by IRF-3 include not only the classical IRF-responsive genes IFNalpha1 and beta but also new candidates such as genes encoding for the chemokine RANTES and the cytokine IL-15.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
Indirect
PMID: 12213596
Genes targeted by IRF-3 include not only the classical IRF-responsive genes IFNalpha1 and beta but also new candidates such as genes encoding for the chemokine RANTES and the cytokine IL-15.
Indirect
PMID: 12213596
Recently, the IFN-stimulated gene ISG56 was shown to be a direct target of IRF-3.
PMID: 12213596, 11118224
Interestingly, ISG56 acts as an inhibitor of cell proliferation by downregulating protein synthesis through interaction with the p48 subunit of eIF-3.
PMID: 12213596, 11118224
Interestingly, ISG56 acts as an inhibitor of cell proliferation by downregulating protein synthesis through interaction with the p48 subunit of eIF-3.
Indirect
PMID: 12213596, 11118224
Thus, the translation inhibitory function of ISG56 may provide, at least in part, a mechanistic explanation for the ability of IRF-3 5D to mediate apoptosis.
Indirect
PMID: 12213596, 11118224
Thus, the translation inhibitory function of ISG56 may provide, at least in part, a mechanistic explanation for the ability of IRF-3 5D to mediate apoptosis.
Indirect
PMID: 12213596
Virus-mediated activation of IRF-3 through VAK is dependent on viral entry and transcription, since replication deficient virus failed to induce IRF-3 activity.
Indirect
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596, 10626894, 10611240, 11846975
Virus infection or dsRNA treatment leads to the activation of the stress-activated members of the MAP kinase (MAP K) superfamily, namely the c-Jun amino terminal kinases (JNKs) and p38 proteins which are downstream of well defined stress-activated kinase cascades comprised of MKK4,7 and MKK3,6 respectively.
Indirect
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596, 10626894, 10611240, 11846975
Virus infection or dsRNA treatment leads to the activation of the stress-activated members of the MAP kinase (MAP K) superfamily, namely the c-Jun amino terminal kinases (JNKs) and p38 proteins which are downstream of well defined stress-activated kinase cascades comprised of MKK4,7 and MKK3,6 respectively.
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596, 10626894, 10611240, 11846975
Virus infection or dsRNA treatment leads to the activation of the stress-activated members of the MAP kinase (MAP K) superfamily, namely the c-Jun amino terminal kinases (JNKs) and p38 proteins which are downstream of well defined stress-activated kinase cascades comprised of MKK4,7 and MKK3,6 respectively.
Indirect
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596, 10626894, 10611240, 11846975
Virus infection or dsRNA treatment leads to the activation of the stress-activated members of the MAP kinase (MAP K) superfamily, namely the c-Jun amino terminal kinases (JNKs) and p38 proteins which are downstream of well defined stress-activated kinase cascades comprised of MKK4,7 and MKK3,6 respectively.
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
Indirect
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596, 10626894, 10611240, 11846975
Virus infection or dsRNA treatment leads to the activation of the stress-activated members of the MAP kinase (MAP K) superfamily, namely the c-Jun amino terminal kinases (JNKs) and p38 proteins which are downstream of well defined stress-activated kinase cascades comprised of MKK4,7 and MKK3,6 respectively.
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
Indirect
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596, 10626894, 10611240, 11846975
Virus infection or dsRNA treatment leads to the activation of the stress-activated members of the MAP kinase (MAP K) superfamily, namely the c-Jun amino terminal kinases (JNKs) and p38 proteins which are downstream of well defined stress-activated kinase cascades comprised of MKK4,7 and MKK3,6 respectively.
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
PMID: 12213596, 11401490
Indeed, PACT, a dsRNA-binding protein originally identified as an activator of PKR, was shown to enhance IRF-3 activation.
PMID: 12213596
Interestingly, N protein physically interacts with IRF-3, implying that IRF-3 itself represents the molecule that detects the viral pathogen via nucleocapsid recognition.
PMID: 12213596, 11907205
Indeed, a recent study has shown that the N nucleocapsid (N) protein of MeV induced IRF-3 activation via the induction of VAK.
PMID: 12213596
Following interaction with dsRNA, PKR becomes autophosphorylated and, in turn, phosphorylates a restricted number of substrates, the best characterized of which is the α subunit of eukaryotic protein synthesis initiation factor 2 (eIF2alpha).
Indirect
PMID: 12213596
Following interaction with dsRNA, PKR becomes autophosphorylated and, in turn, phosphorylates a restricted number of substrates, the best characterized of which is the alpha subunit of eukaryotic protein synthesis initiation factor 2 (eIF2alpha).
PMID: 12213596, 11585785
Phosphorylation of eIF2alpha on Ser 51 causes a dramatic inhibition of protein synthesis by sequestering the guanine nucleotide exchange factor eIF2B, a rate-limiting component of the translation machinery.
PMID: 12213596, 11585785
Phosphorylation of eIF2alpha on Ser 51 causes a dramatic inhibition of protein synthesis by sequestering the guanine nucleotide exchange factor eIF2B, a rate-limiting component of the translation machinery.
PMID: 12213596, 10626894, 10848580
Another putative target of PKR is the IKKbeta subunit of the IKK complex that physically associates with PKR [20] and is believed to mediate the NF-kappaB activation in a manner that is independent of PKR kinase activity.
PMID: 12213596, 10626894, 10848580
Another putative target of PKR is the IKKbeta subunit of the IKK complex that physically associates with PKR [20] and is believed to mediate the NF-kappaB activation in a manner that is independent of PKR kinase activity.
Indirect
PMID: 12213596, 11607032
Activation of TLR-3 induces the activation of both MAPK and NF-kappaB pathways, independently of the adapter protein MyD88.
Indirect
PMID: 12213596, 11477402, 11191641
Indeed, following PAMP interaction with the TLRs, the IKK and JNK/p38 pathways are activated resulting in the activation of NF-kappaB and AP-1 transcription factors which ultimately lead to cytokine production.
Indirect
PMID: 12213596, 11477402, 11191641
Indeed, following PAMP interaction with the TLRs, the IKK and JNK/p38 pathways are activated resulting in the activation of NF-kappaB and AP-1 transcription factors which ultimately lead to cytokine production.
Indirect
PMID: 12213596, 11477402, 11191641
Indeed, following PAMP interaction with the TLRs, the IKK and JNK/p38 pathways are activated resulting in the activation of NF-kappaB and AP-1 transcription factors which ultimately lead to cytokine production.
PMID: 12213596
Activated TLRs associate with a cytoplasmic adapter molecule, MyD88, through the homophilic interaction between their TIR domains.
PMID: 12213596
MyD88 interacts with the Ser/Thr kinase IRAK which subsequently activates the TRAF6 adapter.
PMID: 12213596
MyD88 interacts with the Ser/Thr kinase IRAK which subsequently activates the TRAF6 adapter.
PMID: 12213596
MyD88 interacts with the Ser/Thr kinase IRAK which subsequently activates the TRAF6 adapter.
Indirect
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
PMID: 12213596, 11477402
Treatment of target cells with LPS activates multiple signaling pathways in addition to IKK/JNK/p38, such as protein kinase C, Src-type tyrosine kinases, and the phosphatidylinositol 3-kinase-protein kinase B pathways.
Indirect
PMID: 12213596, 11477402
Treatment of target cells with LPS activates multiple signaling pathways in addition to IKK/JNK/p38, such as protein kinase C, Src-type tyrosine kinases, and the phosphatidylinositol 3-kinase-protein kinase B pathways.
Indirect
PMID: 12213596, 11477402
Treatment of target cells with LPS activates multiple signaling pathways in addition to IKK/JNK/p38, such as protein kinase C, Src-type tyrosine kinases, and the phosphatidylinositol 3-kinase-protein kinase B pathways.
Indirect
PMID: 12213596, 11698465
Phosphorylation of IRF-3 in response to LPS was demonstrated by Akira’s group.
PMID: 12213596, 10678979, 11896392
Treatment of murine macrophages with LPS also induces the production of IFNbeta, suggesting the activation of some IRF members by LPS [4 and 5] and also implying a role for ISGs in response to bacterial infection.
PMID: 1213596, 11854279
Another target gene, called UBP43 was also recently shown to be induced by LPS via IRF-3 in the murine macrophage-like cell line RAW 264.7.
Indirect
PMID: 1213596, 11854279
Another target gene, called UBP43 was also recently shown to be induced by LPS via IRF-3 in the murine macrophage-like cell line RAW 264.7.
Indirect
PMID: 12213596, 11698465
Kim et al. [47] demonstrated that stress inducers and genotoxic agents such as DNA damaging agents doxorubicin and UV radiation stimulated IRF-3 phosphorylation, nuclear translocation, CBP association, and transcriptional activation of an IRF-3 responsive promoter.
PMID: 12213596, 11035028
Phosphorylation of IRF-3 by the DNA damaging agent doxorubicin, by the osmotic shock inducer sorbitol, the stress inducer anisomycin, the phorbol ester PMA and overexpression of the MAP KKK family members MEKK1 and Cot has also been observed with phosphorylation occurring at the N-terminal end, between aa 186–198.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
Indirect
PMID: 12213596, 10747925
In addition, a small molecule CG18 that stimulates MEKK1 activity activated the stress-mediated signaling pathway and stimulated the formation of the IFN-beta enhanceosome [48], including the activation of ATF-2/c-Jun, IRF-3, and NF-kappaB.
Indirect
PMID: 12213596, 10747925
In addition, a small molecule CG18 that stimulates MEKK1 activity activated the stress-mediated signaling pathway and stimulated the formation of the IFN-beta enhanceosome [48], including the activation of ATF-2/c-Jun, IRF-3, and NF-kappaB.
PMID: 12213596
In these studies, MEKK1 activated IRF-3 through the JNK pathway but not through p38 or IKK pathways.
PMID: 12213596, 10747925
However, the phosphorylation site(s) targeted by the MEKK1-related pathway are distinct from the C-terminal sites, since the IRF-3 (5A) protein, in which the five phosphoacceptor sites in the C-terminal end (Ser 396 to Ser 405) were mutated to alanine (see Fig. 2), was still phosphorylated in response to CG18 and MEKK1.
Indirect
PMID: 12213596
TRAF6 in turn activates the stress-related MAPK pathways JNK and p38, as well as the IKK complex leading to AP-1 and NF-kappaB activation respectively, and the induction of cytokines such as TNF-alpha and IL-6.
Indirect
PMID: 12213596
TRAF6 in turn activates the stress-related MAPK pathways JNK and p38, as well as the IKK complex leading to AP-1 and NF-kappaB activation respectively, and the induction of cytokines such as TNF-alpha and IL-6.
Indirect
PMID: 12213596, 10747925
In addition, a small molecule CG18 that stimulates MEKK1 activity activated the stress-mediated signaling pathway and stimulated the formation of the IFN-beta enhanceosome [48], including the activation of ATF-2/c-Jun, IRF-3, and NF-kappaB.
PMID: 12213596
In these studies, MEKK1 activated IRF-3 through the JNK pathway but not through p38 or IKK pathways.
PMID: 12213596
These experiments imply that MEKK1 can induce IRF-3 and ATF2/c-Jun through the JNK pathway and NF-kappaB through the IKK pathway, resulting in the integration of multiple signal transduction pathways leading to the proper assembly of the IFN-beta enhanceosome.
Indirect
PMID: 12213596, 10747925
In addition, a small molecule CG18 that stimulates MEKK1 activity activated the stress-mediated signaling pathway and stimulated the formation of the IFN-beta enhanceosome [48], including the activation of ATF-2/c-Jun, IRF-3, and NF-kappaB.
PMID: 12213596
These experiments imply that MEKK1 can induce IRF-3 and ATF2/c-Jun through the JNK pathway and NF-kappaB through the IKK pathway, resulting in the integration of multiple signal transduction pathways leading to the proper assembly of the IFN-beta enhanceosome.
Indirect
PMID: 12213596
These experiments imply that MEKK1 can induce IRF-3 and ATF2/c-Jun through the JNK pathway and NF-kappaB through the IKK pathway, resulting in the integration of multiple signal transduction pathways leading to the proper assembly of the IFN-beta enhanceosome.
Indirect
PMID: 12213596, 11035028
Phosphorylation of IRF-3 by the DNA damaging agent doxorubicin, by the osmotic shock inducer sorbitol, the stress inducer anisomycin, the phorbol ester PMA and overexpression of the MAP KKK family members MEKK1 and Cot has also been observed with phosphorylation occurring at the N-terminal end, between aa 186–198.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
Indirect
PMID: 12213596, 11035028
Phosphorylation of IRF-3 by the DNA damaging agent doxorubicin, by the osmotic shock inducer sorbitol, the stress inducer anisomycin, the phorbol ester PMA and overexpression of the MAP KKK family members MEKK1 and Cot has also been observed with phosphorylation occurring at the N-terminal end, between aa 186–198.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
Indirect
PMID: 12213596, 11035028
Phosphorylation of IRF-3 by the DNA damaging agent doxorubicin, by the osmotic shock inducer sorbitol, the stress inducer anisomycin, the phorbol ester PMA and overexpression of the MAP KKK family members MEKK1 and Cot has also been observed with phosphorylation occurring at the N-terminal end, between aa 186–198.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
Indirect
PMID: 12213596, 11035028
Phosphorylation of IRF-3 by the DNA damaging agent doxorubicin, by the osmotic shock inducer sorbitol, the stress inducer anisomycin, the phorbol ester PMA and overexpression of the MAP KKK family members MEKK1 and Cot has also been observed with phosphorylation occurring at the N-terminal end, between aa 186–198.
PMID: 12213596, 11035028
Indeed, as opposed to the observation made by Kim’s group, stress-inducers and DNA damaging agents failed to induce nuclear accumulation through CBP association or transcriptional activation of RANTES promoter.
Indirect
PMID: 12213596
DNA-PK phosphorylates Thr 135 near the nuclear export sequence and may inhibit export of IRF-3 from the nucleus.
Indirect
PMID: 12213596, 11698465
Recently, Akira’s group observed induction of the IP-10 gene with lipid A, the functional moiety of LPS, in MyD88-deficient peritoneal macrophages in which production of TNF-alpha and IL-6 in response to LPS is completely impaired.
Indirect
PMID: 12213596, 11401490
Indeed, PACT, a dsRNA-binding protein originally identified as an activator of PKR, was shown to enhance IRF-3 activation.
Indirect
PMID: 12213596, 10626894, 10848580
Another putative target of PKR is the IKKbeta subunit of the IKK complex that physically associates with PKR [20] and is believed to mediate the NF-kappaB activation in a manner that is independent of PKR kinase activity.
Indirect
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
PMID: 12213596
Components of bacterial cell wall, such as LPS, activate TLR4 signaling, leading to cytokine production through the activation of JNK/p38 and IKK complex.
Indirect
PMID: 12213596
Virus infection results in the activation of multiple signaling cascades resulting in the phosphorylation of ATF-2, C-Jun, IRF-3, and NF-kapppaB.
PMID: 12213596
Following virus replication, the generation of dsRNA activates the stress-induced MAPK pathway p38/JNK resulting in the AP-1 activation.
PMID: 12213596
The heterodimers ATF-2/c-Jun are expressed as nuclear proteins that are activated by phosphorylation of their activation domains by p38/JNK.
PMID: 12213596, 10747925
In addition, a small molecule CG18 that stimulates MEKK1 activity activated the stress-mediated signaling pathway and stimulated the formation of the IFN-beta enhanceosome [48], including the activation of ATF-2/c-Jun, IRF-3, and NF-kappaB.
PMID: 12213596
Following interaction with dsRNA, PKR becomes autophosphorylated and, in turn, phosphorylates a restricted number of substrates, the best characterized of which is the alpha subunit of eukaryotic protein synthesis initiation factor 2 (eIF2alpha).
PMID: 12213596, 9566918, 9463386, 10082512
In addition, IRF-3 C-terminal phosphorylation is required for association with the histone acetyltransferase nuclear proteins CBP and p300 [10, 13 and 23] causing IRF-3, which normally shuttles into and out of the nucleus, to become predominantly nuclear.
PMID: 12213596
DNA-PK phosphorylates Thr 135 near the nuclear export sequence and may inhibit export of IRF-3 from the nucleus.