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
Citations
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Targeting Nuclear Factor-Kappa B to Overcome Resistance to Chemotherapy
TL;DR: In this article, the role of NF-κB in cancer and in the development of resistance, particularly cisplatin, was described and the potential benefits and disadvantages of targeting NFκB signaling by pharmacological intervention was addressed.
Journal ArticleDOI
Activation of JAK/STAT pathway transduces cytoprotective signal in rat acute myocardial infarction.
Shinji Negoro,Keita Kunisada,Eiroh Tone,Masanobu Funamoto,Hidemasa Oh,Tadamitsu Kishimoto,Keiko Yamauchi-Takihara +6 more
TL;DR: The JAK/STAT pathway is activated in AMI myocardium and plays a pivotal role in cytoprotective signaling.
Journal ArticleDOI
Serine phosphorylation and negative regulation of Stat3 by JNK.
Cheh Peng Lim,Xinmin Cao +1 more
TL;DR: It is demonstrated that JNK1, activated by its upstream kinase MKK7, negatively regulated the tyrosine phosphorylation and DNA binding and transcriptional activities of Stat3 stimulated by EGF and pretreatment of cells with UV reduced the EGF-stimulated tyrosining and phosphotyrosine-dependent activities of stat3.
Journal ArticleDOI
SOCS3 binds specific receptor–JAK complexes to control cytokine signaling by direct kinase inhibition
Nadia J. Kershaw,James M. Murphy,James M. Murphy,Nicholas P. D. Liau,Nicholas P. D. Liau,Leila N. Varghese,Leila N. Varghese,Artem Laktyushin,Eden L Whitlock,Isabelle S Lucet,Nicos A. Nicola,Nicos A. Nicola,Jeffrey J. Babon,Jeffrey J. Babon +13 more
TL;DR: In this article, the crystal structure of SOCS3 bound to JAK2 and a fragment of the interleulkin-6 receptor reveals how it exerts its inhibitory activity by blocking substrate binding.
References
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Journal ArticleDOI
Stimulation of 3T3 cells induces transcription of the c- fos proto-oncogene
TL;DR: Transcription of the c-fos proto-oncogene is greatly increased within minutes of administering purified growth factors to quiescent 3T3 cells, and this stimulation is the most rapid transcriptional response to peptide growth factors yet described, implying a role for c- fos in cell-cycle control.
Journal ArticleDOI
Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis
Michael Fried,Donald M. Crothers +1 more
TL;DR: Gel electrophoresis in studies of equilibrium binding, site distribution, and kinetics of protein-DNA interactions found that binding to the so-called third operator site (03) is 15-18 fold weaker than operator binding, and that the binding reactions with the first and third operators are uncoupled, implying that there is no communication between the sites.
Journal ArticleDOI
Stat3: a STAT family member activated by tyrosine phosphorylation in response to epidermal growth factor and interleukin-6
TL;DR: A new family member, Stat3, becomes activated through phosphorylation on tyrosine as a DNA binding protein in response to epidermal growth factor and interleukin-6 but not interferon gamma (IFN-gamma).
Journal ArticleDOI
SH2 and SH3 Domains: Elements that Control Interactions of Cytoplasmic Signaling Proteins
TL;DR: Observations suggest that SH2 and SH3 domains participate in the control of intracellular responses to growth factor stimulation.
Journal ArticleDOI
A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system
Mark M. Garner,Arnold Revzin +1 more
TL;DR: It is demonstrated that even when pre-formed in the presence of CAP-cAMP, the polymerase-promoter open complex becomes unstable if CAP is then selectively removed, and this gel method is applied to the study of the E. coli lactose operon regulatory system.
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