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 ![]() | |
Behrmann, Iris ![]() | |
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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