Animals; Phosphorylation; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Protein Tyrosine Phosphatase, Non-Receptor Type 6; Protein Tyrosine Phosphatases; Receptors, Interleukin-6; STAT1 Transcription Factor; STAT3 Transcription Factor; Trans-Activators; Mice; Membrane Glycoproteins; Intracellular Signaling Peptides and Proteins; Antigens, CD; Cell Line; Cytokine Receptor gp130; DNA-Binding Proteins; Endocytosis; Erythropoietin; Humans; Interleukin-6; Tumor Cells, Cultured
Abstract :
[en] The interleukin-6 (IL-6) receptor complex comprises the IL-6 receptor (IL-6R, gp80) and the signal transducer gp130. Binding of IL-6 to its receptor results in dimerization of gp130, activation of the Jak/STAT pathway, and in a down-regulation of IL-6 binding sites by endocytosis. The STAT activation after stimulation is transient, being maximal after 15-30 min and disappearing after 60-90 min. The mechanism which leads to the termination of the signal is still unknown.In this paper we have studied whether the down-modulation of the STAT signal requires the endocytosis of the receptor complex. Our results suggest that the desensitization of the IL-6 signal is not due to internalization of the receptor complex but requires de novo protein synthesis.
Disciplines :
Biochemistry, biophysics & molecular biology
Identifiers :
UNILU:UL-ARTICLE-2008-735
Author, co-author :
Thiel, S.
Sommer, U.
Kortylewski, M.
Haan, Claude ; University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Behrmann, Iris ; University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Heinrich, P. C.
Graeve, L.
Language :
English
Title :
Termination of IL-6-induced STAT activation is independent of receptor internalization but requires de novo protein synthesis
