Association of Transcription Factor APRF and Protein Kinase Jak1 with the Interleukin-6 Signal Transducer gp130
- 7 January 1994
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 263 (5143) , 89-92
- https://doi.org/10.1126/science.8272872
Abstract
Interleukin-6 (IL-6), leukemia inhibitory factor, oncostatin M, interleukin-11, and ciliary neurotrophic factor bind to receptor complexes that share the signal transducer gp130. Upon binding, the ligands rapidly activate DNA binding of acute-phase response factor (APRF), a protein antigenically related to the p91 subunit of the interferon-stimulated gene factor-3α (ISGF-3α). These cytokines caused tyrosine phosphorylation of APRF and ISGF-3α p91. Protein kinases of the Jak family were also rapidly tyrosine phosphorylated, and both APRF and Jak1 associated with gp130. These data indicate that Jak family protein kinases may participate in IL-6 signaling and that APRF may be activated in a complex with gp130.Keywords
This publication has 22 references indexed in Scilit:
- Induction by EGF and Interferon-γ of Tyrosine Phosphorylated DNA Binding Proteins in Mouse Liver NucleiScience, 1993
- Transcription factor p91 interacts with the epidermal growth factor receptor and mediates activation of the c-fos gene promoterCell, 1993
- The alphas, betas, and kinases of cytokine receptor complexesCell, 1993
- Identification of JAK2 as a growth hormone receptor-associated tyrosine kinaseCell, 1993
- JAK2 associates with the erythropoietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietinCell, 1993
- IL-6-Induced Homodimerization of gp130 and Associated Activation of a Tyrosine KinaseScience, 1993
- Interferon-Dependent Tyrosine Phosphorylation of a Latent Cytoplasmic Transcription FactorScience, 1992
- A protein tyrosine kinase in the interferon αβ signaling pathwayCell, 1992
- Molecular cloning and expression of an IL-6 signal transducer, gp130Cell, 1990
- Interferon-alpha regulates nuclear translocation and DNA-binding affinity of ISGF3, a multimeric transcriptional activator.Genes & Development, 1990