Reference : Termination of IL-6-induced STAT activation is independent of receptor internalizatio...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/6256
Termination of IL-6-induced STAT activation is independent of receptor internalization but requires de novo protein synthesis
English
Thiel, S. [> >]
Sommer, U. [> >]
Kortylewski, M. [> >]
Haan, Claude mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Behrmann, Iris mailto [University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit >]
Heinrich, P. C. [> >]
Graeve, L. [> >]
2000
FEBS Letters
Elsevier Science
470
1
15-9
Yes (verified by ORBilu)
International
0014-5793
Amsterdam
The Netherlands
[en] 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
[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.
http://hdl.handle.net/10993/6256

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