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PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
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PMID: 18800159
mTOR associates with the adaptor proteins raptor and LST8 (GβL) to form a complex called ‘mTORC1’ that initiates translation by phosphorylating members of
at least two families of translational modulators, the p70 ribosomal S6 kinases (S6Ks)1 and 2 (S6K1,2) and the eIF4E-binding proteins (4E-BPs).
PMID: 18800159
In the second mechanism, rapamycin treatment disrupts mTOR-raptor interaction, which prevents mTOR from phosphorylating 4E-BPs.
PMID: 18800159
mTOR associates with the adaptor proteins raptor and LST8 (GβL) to form a complex called ‘mTORC1’ that initiates translation by phosphorylating members of
at least two families of translational modulators, the p70 ribosomal S6 kinases (S6Ks)1 and 2 (S6K1,2) and the eIF4E-binding proteins (4E-BPs).
PMID: 18800159
Pulendran and colleagues now show that phosphorylation of mTOR, 4E-BPs and S6Ks in response to TLR9 activation is blocked by the highly specific drug rapamycin, a macrolide that, in a complex with the immunophilin FKBP12, binds to mTORC1 and inhibits mTORC1 activity
PMID: 18800159
mTOR associates with the adaptor proteins raptor and LST8 (GβL) to form a complex called ‘mTORC1’ that initiates translation by phosphorylating members of
at least two families of translational modulators, the p70 ribosomal S6 kinases (S6Ks)1 and 2 (S6K1,2) and the eIF4E-binding proteins (4E-BPs).
PMID: 18800159
Pulendran and colleagues now show that phosphorylation of mTOR, 4E-BPs and S6Ks in response to TLR9 activation is blocked by the highly specific drug rapamycin, a macrolide that, in a complex with the immunophilin FKBP12, binds to mTORC1 and inhibits mTORC1 activity
PMID: 18800159
mTOR associates with the adaptor proteins raptor and LST8 (GβL) to form a complex called ‘mTORC1’ that initiates translation by phosphorylating members of
at least two families of translational modulators, the p70 ribosomal S6 kinases (S6Ks)1 and 2 (S6K1,2) and the eIF4E-binding proteins (4E-BPs).
PMID: 18800159
Pulendran and colleagues now show that phosphorylation of mTOR, 4E-BPs and S6Ks in response to TLR9 activation is blocked by the highly specific drug rapamycin, a macrolide that, in a complex with the immunophilin FKBP12, binds to mTORC1 and inhibits mTORC1 activity
PMID: 18800159
4E-BPs (of which three forms exist in mammals) inhibit translation by binding the cap-binding protein eIF4E
PMID: 18800159
4E-BPs (of which three forms exist in mammals) inhibit translation by binding the cap-binding protein eIF4E
PMID: 18800159
the S6Ks phosphorylate and activate (among other substrates) eIF4B, a translation-initiation factor.
PMID: 18800159
the S6Ks phosphorylate and activate (among other substrates) eIF4B, a translation-initiation factor.
indirect
PMID: 18800159
the TLR9 ligand CpG-A triggers rapid phosphorylation of mTOR and its ‘downstream’ targets 4E-BPs and S6Ks.
indirect
PMID: 18800159
the TLR9 ligand CpG-A triggers rapid phosphorylation of mTOR and its ‘downstream’ targets 4E-BPs and S6Ks.
indirect
PMID: 18800159
the TLR9 ligand CpG-A triggers rapid phosphorylation of mTOR and its ‘downstream’ targets 4E-BPs and S6Ks.
indirect
PMID: 18800159
the TLR9 ligand CpG-A triggers rapid phosphorylation of mTOR and its ‘downstream’ targets 4E-BPs and S6Ks.
PMID: 18800159
Pulendran and colleagues now show that phosphorylation of mTOR, 4E-BPs and S6Ks in response to TLR9 activation is blocked by the highly specific drug rapamycin, a macrolide that, in a complex with the immunophilin FKBP12, binds to mTORC1 and inhibits mTORC1 activity
PMID: 18800159
Pulendran and colleagues now show that phosphorylation of mTOR, 4E-BPs and S6Ks in response to TLR9 activation is blocked by the highly specific drug rapamycin, a macrolide that, in a complex with the immunophilin FKBP12, binds to mTORC1 and inhibits mTORC1 activity
PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
indirect
PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
indirect
PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
indirect
PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
indirect
PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
indirect
PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
indirect
PMID: 18800159
both TLR7- and TLR9-mediated production of type I interferon, tumor necrosis factor and interleukin 6 (IL-6) is suppressed in human and mouse pDCs treated with rapamycin.
PMID: 18800159
The effect of rapamycin is not limited to pDCs, as the production of IL-10, IL-6 and tumor necrosis factor is also impaired in bone marrow– derived DCs treated with rapamycin
indirect
PMID: 18800159
they find that a decrease in S6K activity resulting from the use of rapamycin or siRNA specific for S6K1,2 impedes the production of type I interferon and formation of the TLR9-MyD88 complex.
PMID: 18800159
S6K phosphorylation mediated by mTOR promotes formation of the TLR9-MyD88 complex
PMID: 18800159
The interaction of TLR with MyD88 in pDCs elicits the formation of multifactor signaling transduction complex that contains the kinases IRAK1 and IRAK4, the ubiquitin ligase TRAF6, the tyrosine kinase BTK and IRF7
PMID: 18800159, 18641647
IRF7 is phosphorylated by IRAK1- IRAK4 and then translocates to the nucleus, where it initiates the transcription of genes encoding type I interferons
PMID: 18800159, 18641647
IRF7 is phosphorylated by IRAK1- IRAK4 and then translocates to the nucleus, where it initiates the transcription of genes encoding type I interferons
PMID: 18800159, 18641647
IRF7 is phosphorylated by IRAK1- IRAK4 and then translocates to the nucleus, where it initiates the transcription of genes encoding type I interferons
indirect
PMID: 18800159
the expression of a subset of genes encoding interferons and cytokines such as interferon-α4, interferon-β1, IFI44, IFI202B, CCL7, CCL8 and CCL12 is induced by CpG-A but is repressed by rapamycin.
indirect
PMID: 18800159
the expression of a subset of genes encoding interferons and cytokines such as interferon-α4, interferon-β1, IFI44, IFI202B, CCL7, CCL8 and CCL12 is induced by CpG-A but is repressed by rapamycin.
indirect
PMID: 18800159
the expression of a subset of genes encoding interferons and cytokines such as interferon-α4, interferon-β1, IFI44, IFI202B, CCL7, CCL8 and CCL12 is induced by CpG-A but is repressed by rapamycin.
indirect
PMID: 18800159
the expression of a subset of genes encoding interferons and cytokines such as interferon-α4, interferon-β1, IFI44, IFI202B, CCL7, CCL8 and CCL12 is induced by CpG-A but is repressed by rapamycin.
indirect
PMID: 18800159
the expression of a subset of genes encoding interferons and cytokines such as interferon-α4, interferon-β1, IFI44, IFI202B, CCL7, CCL8 and CCL12 is induced by CpG-A but is repressed by rapamycin.
indirect
PMID: 18800159
the expression of a subset of genes encoding interferons and cytokines such as interferon-α4, interferon-β1, IFI44, IFI202B, CCL7, CCL8 and CCL12 is induced by CpG-A but is repressed by rapamycin.
indirect
PMID: 18800159
the expression of a subset of genes encoding interferons and cytokines such as interferon-α4, interferon-β1, IFI44, IFI202B, CCL7, CCL8 and CCL12 is induced by CpG-A but is repressed by rapamycin.
PMID: 18800159
The mTOR-dependent phophorylation of 4 E-BPs results in low-affinity binding to eIF4E and thus elicit more translation of IRF7 mRNA.
PMID: 18800159, 18272964
One of these mRNAs, IRF7, has been shown to be translationally controlled by 4E-BPs and is responsible for the enhanced production of type I interferon and virus-resistant phenotype of MEFs doubly deficient in 4E-BP1 and 4E-BP2.
PMID: 18800159
hypophosphorylated 4E-BPs then bind to the cap-binding protein eIF4E with high affinity, thus decreasing the translation of a subset of mRNAs.