scispace - formally typeset
Journal ArticleDOI

Jak-STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins

Reads0
Chats0
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
More filters
Journal ArticleDOI

Characterization of β-R1, a Gene That Is Selectively Induced by Interferon β (IFN-β) Compared with IFN-α

TL;DR: Induction of the β-R1 gene in fibrosarcoma cells and derivative mutant cells lacking components required for signaling by type I IFNs requires IFN-stimulated gene factor 3 plus an additional component, which is more efficiently formed on induction by IFn-β compared withIFN-α.
Journal ArticleDOI

Interferons: mechanisms of action and clinical applications.

TL;DR: An update on basic and clinical research in the interferon field is provided, and potential translational applications, reflecting recent advances in the field, are discussed.
Journal ArticleDOI

STAT3 mediates IL-6-induced neuroendocrine differentiation in prostate cancer cells .

TL;DR: This work investigated whether STAT3 also mediated NE differentiation in this prostate cancer cell line and observed that IL‐6 mediated growth arrest in LNCaP by activating STAT 3.
Journal ArticleDOI

The erythropoietin receptor cytosolic juxtamembrane domain contains an essential, precisely oriented, hydrophobic motif.

TL;DR: It is reported that the erythropoietin receptor cytosolic juxtamembrane region is conformationally rigid and contains a hydrophobic motif that is crucial for Janus kinase 2 (JAK2) activation and receptor signaling.
Journal ArticleDOI

The long form of the leptin receptor regulates STAT5 and ribosomal protein S6 via alternate mechanisms.

TL;DR: It is demonstrated that leptin stimulates the phosphorylation of STAT5 and ribosomal protein S6 in the hypothalamic arcuate nucleus in mice, and the mechanisms by which leptin regulates each of these signals and their effects in cultured cells are investigated.
References
More filters
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

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

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.
Related Papers (5)