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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What does Stat3 do
David E. Levy,Chien-Kuo Lee +1 more
TL;DR: Recent data, especially from the analysis of conditional loss of Stat3 protein in adult tissues, confirm that Stat3 participates in a wide variety of physiological processes and even directs seemingly contradictory responses.
Journal ArticleDOI
Mutations of Jak-3 gene in patients with autosomal severe combined immune deficiency (SCID).
Paolo Macchi,Anna Villa,Silvia Giliani,Maria Grazia Sacco,Annalisa Frattini,Fulvio Porta,A. G. Ugazio,J A Johnston,Fabio Candotti,John J. O'Shea +9 more
TL;DR: Two unrelated T- B+SCID patients who have homozygous mutations in the gene for Jak-3 are investigated and abnormalities in the Jak/STAT signalling pathway can account for SCID in humans.
Journal ArticleDOI
Integration of interferon-alpha/beta signalling to p53 responses in tumour suppression and antiviral defence.
Akinori Takaoka,Sumio Hayakawa,Hideyuki Yanai,Dagmar Stoiber,Dagmar Stoiber,Hideo Negishi,Hideaki Kikuchi,Shigeru Sasaki,Kohzoh Imai,Tsukasa Shibue,Kenya Honda,Tadatsugu Taniguchi +11 more
TL;DR: It is shown that transcription of the p53 gene is induced by IFN-α/β, accompanied by an increase in p53 protein level, and that p53 is critical for antiviral defence of the host.
Journal ArticleDOI
Jak2 Deficiency Defines an EssentialDevelopmental Checkpoint in DefinitiveHematopoiesis
TL;DR: The data provided demonstrate that Jak2 has pivotal functions for signal transduction of a set of cytokine receptors required in definitive erythropoiesis.
Journal ArticleDOI
An interleukin-4-induced transcription factor: IL-4 Stat
TL;DR: Examination of the primary amino acid sequence of this protein indicates that it is a member of the signal transducers and activators of transcription (Stat) family of DNA binding proteins, hereby designated IL-4 Stat, and indicates that IL- 4 Stat has the same functional domain for both receptor coupling and dimerization.
References
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Journal ArticleDOI
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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
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