Journal ArticleDOI
Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins
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TLDR
A previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that phosphorylate substrate proteins called STATs (signal transducers and activators of transcription).Abstract:
Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.read more
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Nucleocytoplasmic shuttling by nucleoporins Nup153 and Nup214 and CRM1-dependent nuclear export control the subcellular distribution of latent Stat1.
TL;DR: It is proposed that two independent translocation pathways cooperate to determine the steady-state distribution of Stat1, and it is revealed that constitutive nucleocytoplasmic shuttling of Stat 1 is mediated by direct interactions with the FG repeat regions of nucleoporin 153 and nucleoparin 214 of the nuclear pore.
Journal ArticleDOI
Galectin-3 Exerts Cytokine-Like Regulatory Actions through the JAK–STAT Pathway
TL;DR: It is shown that galectin-3 exerts cytokine-like regulatory actions in rat and mouse brain-resident immune cells and significantly induced phosphorylation of STATs in glial cells from IFN–γ–deficient mice, suggesting that IFN-γ does not mediate activation ofSTATs.
Journal ArticleDOI
Enhancement of antiproliferative activity of gamma interferon by the specific inhibition of tyrosine dephosphorylation of Stat1.
Ke Shuai,Jiayu Liao,M M Song +2 more
TL;DR: It is suggested that the N-terminal domains ofSTATs are crucial for modulating STAT activities through regulating the tyrosine dephosphorylation of STATs.
Journal ArticleDOI
Mining for JAK-STAT mutations in cancer.
TL;DR: The Janus kinase-signal transducer and activator of transcription pathway mediates signaling by cytokines, which control survival, proliferation and differentiation of several cell types, and recent discoveries suggest that mutated JAK proteins will be potent targets for anti-cancer therapy.
Journal Article
Inhibition of interferon gamma signaling by the short chain fatty acid butyrate.
TL;DR: Butyrate negatively regulates mucosal inflammation through the inhibition of IFN-;/STAT1 signaling, and abnormal activity of STAT1 is associated with human malignancies and intestinal inflammatory diseases.
References
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Journal ArticleDOI
Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
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Journal ArticleDOI
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
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Journal ArticleDOI
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