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multiprotein complex containing heat shock proteins (hsp90, hsp70), co-chaperones and immunofillins. Ligand binding induces a series of conformational changes in the receptor that result in rearrangement of this complex, exposure of the GR nuclear localization signal and rapid nuclear translocation. PMID: 17576036, 10099820 In its inactive state, GR resides in the cytoplasm as a part of a large multiprotein complex containing heat shock proteins (hsp90, hsp70), co-chaperones and immunofillins. Ligand binding induces a series of conformational changes in the receptor that result in rearrangement of this complex, exposure of the GR nuclear localization signal and rapid nuclear translocation. PMID: 17576036 Simple GREs contain a specific DNA sequence to which GR binds as a sole regulator, typically as a homodimer. PMID: 17576036, 17559307, 9582068 GREs have been proposed to serve as the second ‘allosteric ligand’ for the receptor. Indirect PMID: 17576036, 8455596, 2884660, 2038339 Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription. Indirect PMID: 17576036, 8455596, 2884660, 2038339 Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription. Indirect PMID: 17576036, 8455596, 2884660, 2038339 Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription. Indirect PMID: 17576036, 8455596, 2884660, 2038339 Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription. Indirect PMID: 17576036, 8455596, 2884660, 2038339 Depending on promoter organization, simple GREs could confer either activation (sgk1; tyrosine hydroxylase; chromogranin A) or repression of transcription. PMID: 17576036, 2169352, 10995388, 9388192 Tethering GREs do not contain bona fide DNA recognition sequence for GR, but rather a binding site for another transcription factor which recruits GR through protein:protein interactions. Binding to tethering GREs often requires neither GR DNA binding activity nor its dimerization. Several transcription factors, including AP1, NFkappaB, Stat3 and Stat5 can provide a “tether” for GR. PMID: 17576036, 2169352, 10995388, 9388192 Tethering GREs do not contain bona fide DNA recognition sequence for GR, but rather a binding site for another transcription factor which recruits GR through protein:protein interactions. Binding to tethering GREs often requires neither GR DNA binding activity nor its dimerization. Several transcription factors, including AP1, NFkappaB, Stat3 and Stat5 can provide a “tether” for GR. PMID: 17576036, 2169352, 10995388, 9388192 Tethering GREs do not contain bona fide DNA recognition sequence for GR, but rather a binding site for another transcription factor which recruits GR through protein:protein interactions. Binding to tethering GREs often requires neither GR DNA binding activity nor its dimerization. Several transcription factors, including AP1, NFkappaB, Stat3 and Stat5 can provide a “tether” for GR. PMID: 17576036, 16751179, 15957004, 12215713 the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3. PMID: 17576036, 16751179, 15957004, 12215713 the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3. PMID: 17576036, 16751179, 15957004, 12215713 the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3. PMID: 17576036 GR and IRF3 hinder each other's binding to GRIP1 in vitro suggesting that interacting surfaces may partially overlap precluding GR and IRF3 from binding GRIP1 at the same time. PMID: 17576036, 16751179, 15957004, 12215713 the best understood interaction is that between the GR AF2 and the p160 family members: SRC1, SRC2/GRIP1/TIF2 and SRC3/AIB1/ACTR/Rac3. PMID: 17576036, 14966289, 14690606, 15988012 Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57. PMID: 17576036, 14966289, 14690606, 15988012 Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57. PMID: 17576036, 14966289, 14690606, 15988012 Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57. PMID: 17576036, 14966289, 14690606, 15988012 Although no DNA binding activity has been reported for p160 cofactors, bHLH/PAS domain reportedly binds several secondary coactivators such as flightless I, CoCoA, GAC63 and a component of SWI/SNF chromatin remodeling complex, BAF57. PMID: 17576036, 9430642, 11997499, 15731352 The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively. PMID: 17576036, 9430642, 11997499, 15731352 The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively. PMID: 17576036, 9430642, 11997499, 15731352 The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively. PMID: 17576036, 9430642, 11997499, 15731352 The C-terminal half of p160s houses activation domains (AD) 1 and 2 which recruit histone acetyl transferases (CBP/p300 and pCAF) and arginine methyl transferases (CARM1 and PRMT1), respectively. PMID: 17576036, 10817756, 15767262, 15169882 Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs. PMID: 17576036, 10817756, 15767262, 15169882 Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs. PMID: 17576036, 10817756, 15767262, 15169882 Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs. PMID: 17576036, 10817756, 15767262, 15169882 Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs. PMID: 17576036, 10817756, 15767262, 15169882 Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs. PMID: 17576036, 10817756, 15767262, 15169882 Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs. PMID: 17576036, 10817756, 15767262, 15169882 Historically identified as nuclear receptor coactivators, individual p160s are emerging as cofactors for a variety of non-receptor transcriptional regulators including MEF2C and myogenin, pRb, E2F1, MyoD, NFkappaB, STATs and most recently, IRFs. PMID: 17576036 Ligand-dependent homo- or heterodimerization of TLRs brings two TIR domains in close proximity allowing for the recruitment of additional adaptor molecules. PMID: 17576036 Ligand-dependent homo- or heterodimerization of TLRs brings two TIR domains in close proximity allowing for the recruitment of additional adaptor molecules. PMID: 17576036 Upon interaction with PAMPs, TLRs recruit adaptor proteins MyD88 and TRIF/TICAM1, which transmit signal to downstream kinases as well as ubuiquitin ligases involved in degradation of inhibitors of NFkappaB. PMID: 17576036 Two additional adaptor proteins, TIRAP and TRAM, likely facilitate the recruitment of MyD88 and TRIF to specific TLRs. PMID: 17576036 Upon interaction with PAMPs, TLRs recruit adaptor proteins MyD88 and TRIF/TICAM1, which transmit signal to downstream kinases as well as ubuiquitin ligases involved in degradation of inhibitors of NFkappaB. PMID: 17576036 Two additional adaptor proteins, TIRAP and TRAM, likely facilitate the recruitment of MyD88 and TRIF to specific TLRs. PMID: 17576036 MyD88 contains two protein:protein interaction domains: the C-terminal TIR domain interacts with TIR domain of TLRs and IL-1R, while the N-terminal death domain binds the death domain-containing protein kinases, such as the IL-1R-associated kinase 4 (IRAK4), which phosphorylate another kinase, IRAK1. PMID: 17576036 MyD88 contains two protein:protein interaction domains: the C-terminal TIR domain interacts with TIR domain of TLRs and IL-1R, while the N-terminal death domain binds the death domain-containing protein kinases, such as the IL-1R-associated kinase 4 (IRAK4), which phosphorylate another kinase, IRAK1. PMID: 17576036 The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1. PMID: 17576036 The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1. PMID: 17576036 The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1. PMID: 17576036 The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1. PMID: 17576036 The latter binds to and phosphorylates TRAF6, a ubiquitin ligase that targets TGF-activated kinase (TAK)1. Indirect PMID: 17576036, 16186825, 16260493 Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways. Indirect PMID: 17576036, 16186825, 16260493 Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways. Indirect PMID: 17576036, 16186825, 16260493 Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways. Indirect PMID: 17576036, 16186825, 16260493 Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways. Indirect PMID: 17576036, 16186825, 16260493 Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways. PMID: 17576036, 9407028, 9794429 glucocorticoids inhibit several TLR-activated protein kinases including JNK and p38 without altering their levels, suggesting that GR does not repress transcription of JNK or p38. PMID: 17576036, 16186825, 16260493 Activated TAK1 in turn initiates a cascade of phosphorylation events ultimately inducing the IkappaB kinase (IKK) and the MKK3,4,6/JNK/p38 pathways. PMID: 17576036, 9407028, 9794429 glucocorticoids inhibit several TLR-activated protein kinases including JNK and p38 without altering their levels, suggesting that GR does not repress transcription of JNK or p38. Indirect PMID: 17576036 The former activates transcription factor NFkappaB through the phosphorylation and degradation of its inhibitor, IkappaB, while the latter is involved in numerous stress-related pathways including activation of transcription factors from the AP1 family. PMID: 17576036 The former activates transcription factor NFkappaB through the phosphorylation and degradation of its inhibitor, IkappaB, while the latter is involved in numerous stress-related pathways including activation of transcription factors from the AP1 family. Indirect PMID: 17576036 The former activates transcription factor NFkappaB through the phosphorylation and degradation of its inhibitor, IkappaB, while the latter is involved in numerous stress-related pathways including activation of transcription factors from the AP1 family. PMID: 17576036, 16720699 In TLR3, two positively charged patches (patch1 and patch2) were proposed to be involved in interaction with dsRNA as substitution of either of these patches with alanines abolishes TLR3 signaling. PMID: 17576036, 12471095 TLR3 is the only TLR which does not interact with MyD88 and utilizes another TIR-domain adaptor, TRIF. PMID: 17576036, 16822173, 12692549 The N-terminal domain of TRIF interacts with IRF3 and several kinases including IKK-related TBK1 and IKKepsilon. Indirect PMID: 17576036 TBK1/IKKepsilon phosphorylate IRF3 and possibly IRF7 leading to dimerization and nuclear translocation of these transcription factors. PMID: 17576036 TBK1/IKKepsilon phosphorylate IRF3 and possibly IRF7 leading to dimerization and nuclear translocation of these transcription factors. PMID: 17576036 TBK1/IKKepsilon phosphorylate IRF3 and possibly IRF7 leading to dimerization and nuclear translocation of these transcription factors. PMID: 17576036 The C-terminal domain of TRIF interacts with protein kinase RIP1. Indirect PMID: 17576036, 17073741 Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs). Indirect PMID: 17576036, 17073741 Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs). Indirect PMID: 17576036, 17073741 Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs). Indirect PMID: 17576036, 17073741 Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs). PMID: 17576036, 17073741 Negative regulation of these pathways involves dephosphorylation of JNK, p38 and their upstream kinases MEK3,4,6 by MAPK phosphatases (MKPs, also known as DUSPs). PMID: 17576036, 15032587 These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation. PMID: 17576036, 15032587 These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation. PMID: 17576036, 16415872 Recently, SOCS1 was reported to also directly interfere with TLR 2 and 4 signaling by inducing rapid degradation of their TIR domain-containing adaptor TIRAP through ubiquitin-mediated proteolysis. Indirect PMID: 17576036, 16415872 Recently, SOCS1 was reported to also directly interfere with TLR 2 and 4 signaling by inducing rapid degradation of their TIR domain-containing adaptor TIRAP through ubiquitin-mediated proteolysis. PMID: 17576036, 15032587 These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation. PMID: 17576036, 15032587 These proteins contain SH2 domains which physically interact with JAKs competitively blocking their interaction with STATs as well as serve as adapters for E3 ubiquitin ligases which target JAKs for degradation. Indirect PMID: 17576036, 11259387, 12054511, 16293608 Interestingly, SOCS1 mRNA is induced by glucocorticoids in several cell lines of hematopoietic origin and in acute lymphoblastic leukemia (ALL) patients. Indirect Indirect PMID: 17576036, 11468175, 9430225, 17208592 Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X. PMID: 17576036, 11028557, 11160251, 11867630 Transcription of the TLR2 gene in response to TLR agonists is activated by NFkappaB and could therefore be expected to be glucocorticoid-sensitive. PMID: 17576036 In HeLa cervical carcinoma cells, the basal TLR2 expression is low but is induced upon exposure to lipoprotein from the Gram-negative bacterium Haemophilus influenzae and further potentiated by glucocorticoids. PMID: 17576036,16765091 in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block. PMID: 17576036, 11468175, 9430225, 17208592 Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X. PMID: 17576036, 11468175, 11397794 GILZ was reported to physically interact with several effectors of TLR signaling, most notably Fos, Jun and p65/RelA. PMID: 17576036, 17169985, 11397794, 12391160 Interestingly, GILZ homodimerization through the leucine zipper domain is required for its interaction with NFkappaB, but not AP1 or Raf-1, suggesting that GILZ interaction surfaces are partner-specific. PMID: 17576036, 12391160 In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2. PMID: 17576036, 12391160 In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2. Indirect PMID: 17576036, 12391160 In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2. PMID: 17576036, 12391160 In addition, GILZ binds to the protein kinase Raf-1 blocking its phosphorylation and, consequently, activation of downstream MAPKs, Erk 1 and 2. PMID: 17576036, 11468175, 11397794 GILZ was reported to physically interact with several effectors of TLR signaling, most notably Fos, Jun and p65/RelA. PMID: 17576036, 11468175, 11397794 GILZ was reported to physically interact with several effectors of TLR signaling, most notably Fos, Jun and p65/RelA. PMID: 17576036, 17169985, 11397794, 12391160 Interestingly, GILZ homodimerization through the leucine zipper domain is required for its interaction with NFkappaB, but not AP1 or Raf-1, suggesting that GILZ interaction surfaces are partner-specific. Indirect PMID: 17576036, 11259387, 9430225, 12393603 GILZ is dramatically induced by glucocorticoids in a wide range of cell types, and this induction requires the GR dimer interface and DNA binding, suggesting that GILZ is a direct transcriptional target for the receptor. PMID: 17576036, 12356755 ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists. Indirect PMID: 17576036, 12356755 ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists. Indirect PMID: 17576036, 12356755 ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1beta in response to TLR2 agonists. PMID: 17576036,16765091 in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block. Indirect PMID: 17576036, 12356755 ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists. Indirect PMID: 17576036, 12356755 ectopic overexpression of TLR2 in HeLa cells indeed results in elevated transcription of TNF-alpha, IL-8 and IL-1β in response to TLR2 agonists. Indirect Indirect PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. PMID: 17576036,16765091 in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block. Indirect PMID: 17576036,16765091 in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block. Indirect Indirect PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. Indirect Indirect PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. Indirect Indirect PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. Indirect Indirect PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. Indirect Indirect PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. Indirect Indirect PMID: 17576036, 15242847 Similarly, in the A549 lung epithelial cell line, the induction of IL-6 and IL-8 by TLR2 agonist peptidoglycan is enhanced by co-treatment with TNF-alpha, IFNgamma and glucocorticoid. PMID: 17576036, 16932750 This phosphorylation is required for nuclear translocation of IRF3 as well as binding of CBP/p300, the best known IRF3 coactivators. PMID: 17576036 GR and IRF3 hinder each other's binding to GRIP1 in vitro suggesting that interacting surfaces may partially overlap precluding GR and IRF3 from binding GRIP1 at the same time. PMID: 17576036 both GRIP1 and IRF3 are conventional interacting partners for CBP/p300, their interaction with each other is CBP-independent. Indirect PMID: 17576036 glucocorticoids strongly inhibited dsRNA-induced expression of multiple cytokines and chemokines including interferon beta, IP10 and RANTES, known transcriptional targets of IRF3. Indirect PMID: 17576036 glucocorticoids strongly inhibited dsRNA-induced expression of multiple cytokines and chemokines including interferon beta, IP10 and RANTES, known transcriptional targets of IRF3. Indirect PMID: 17576036 glucocorticoids strongly inhibited dsRNA-induced expression of multiple cytokines and chemokines including interferon beta, IP10 and RANTES, known transcriptional targets of IRF3. PMID: 17576036 both GRIP1 and IRF3 are conventional interacting partners for CBP/p300, their interaction with each other is CBP-independent. PMID: 17576036 TLR4 is the main LPS sensor that can activate IRF3 through both MyD88- and TRIF-dependent pathways. Indirect PMID: 17576036, 10094406 casein kinase II-dependent phosphorylation of IRF1 is required for its full transactivation. PMID: 17576036, 16143103 because both GR and IRF3 appear to interact with the Rel domain of p65, IRF3 and GR were proposed to compete for the same binding site on NFkappaB. PMID: 17576036, 11468175 IRAK4/1 initiate signaling cascades that lead to the activation of NFkappaB, AP1 and possibly IRF7 and IRF5. PMID: 17576036 Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain. PMID: 17576036 Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain. PMID: 17576036 Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain. PMID: 17576036 Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain. PMID: 17576036 Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain. PMID: 17576036 Several IRFs, including IRF1, 2, 3, 5 and 7 interact with CBP/p300 coactivators through the C-terminal IAD domain. PMID: 17576036, 11468175, 9430225, 17208592 Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X. PMID: 17576036 In HeLa cervical carcinoma cells, the basal TLR2 expression is low but is induced upon exposure to lipoprotein from the Gram-negative bacterium Haemophilus influenzae and further potentiated by glucocorticoids. PMID: 17576036,16765091 in dendritic cells, glucocorticoids augment the expression of both TLR2 and TLR4, but inhibit the production of proinflammatory cytokines TNF-alpha and IL-12 in response to TLR agonists, suggesting that TLR2 signaling is blocked downstream of the receptor and that a mere increase in the amount of TLR2 does not relieve this block. PMID: 17576036, 11468175, 9430225, 17208592 Glucocorticoid-inducible leucine zipper (GILZ) is a small protein with a wide spectrum of anti-inflammatory activities including inhibition of LPS-induced expression of TLR2 in macrophages and of TLR 2- and 3-mediated NFkappaB activation in airway epithelial cells; inhibition of dendritic cells’ maturation, and enhancement of spontaneous thymocyte apoptosis, likely through downregulation of the anti-apoptotic factor Bcl-X.