Signaling through a novel domain of gp130 mediates cell proliferation and activation of Hck and Erk kinases.

Interleukin-6 (IL-6) induces the activation of the Src family kinase Hck, which is associated with the IL-6 receptor beta-chain, gp130. Here we describe the identification of an "acidic" domain comprising amino acids 771 to 811 of gp130 as a binding region for Hck, which mediates proliferative signaling. The deletion of ...
this region of gp130 (i.e., in deletion mutant d771-811) resulted in a significant reduction of Hck kinase activity and cell proliferation upon stimulation of gp130 compared to wild-type gp130. In addition, d771-811 disrupted the growth factor-stimulated activation of Erk and the dephosphorylation of Pyk2. Based on these findings, we propose a novel, acidic domain of gp130, which is responsible for the activation of Hck, Erk, and Pyk2 and signals cell proliferation upon growth factor stimulation.
Mesh Terms:
Amino Acid Motifs, Animals, Antigens, CD, Cell Division, Cell Line, Cytokine Receptor gp130, DNA-Binding Proteins, Enzyme Activation, Enzyme Inhibitors, Focal Adhesion Kinase 2, Growth Substances, Humans, Interleukin-6, Membrane Glycoproteins, Mice, Mitogen-Activated Protein Kinases, Mutagenesis, Site-Directed, Protein Binding, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-hck, Receptors, Erythropoietin, Recombinant Fusion Proteins, STAT3 Transcription Factor, Signal Transduction, Trans-Activators, Transfection
Mol. Cell. Biol.
Date: Dec. 01, 2001
Download Curated Data For This Publication
4030
Switch View:
  • Interactions 1