Publikationsserver der RWTH Aachen University
Repression der IL-6-Signaltransduktion über das zytoplasmatische Tyrosin 759 des Signaltransduktors gp130
Abstract
dc:descriptionThis study revealed that tyrosine motifs of gp130 which have been described to recruit STAT-proteins are not equivalent in respect to their potential to activate STAT-factors, acute-phase protein gene promoters and in induction of proliferation. To investigate the potential of each tyrosine-motif add-back-receptor mutants were generated, which contain only one tyrosine-residue and analysed for their contribution in interleukin-6 signal transduction Three families of proteins involved in the down-regulation of cytokine signaling have been described recently: (i) SH2 domain containing protein tyrosine phosphatases (SHP), (ii) suppressors of cytokine signaling (SOCS) and (iii) protein inhibitors of activated STATs (PIAS). We have analyzed the interplay of two inhibitors in the signal transduction pathway of interleukin-6 and demonstrate that the tyrosine phosphatase SHP2 and SOCS3 do not act independently, but are functionally linked. Furthermore, we show that tyrosine 759 in gp130 is essential for both SHP2 and SOCS3, but not for SOCS1 to exert their inhibitory activities on interleukin-6 signal transduction. Besides SHP2 also SOCS3 interacts with a peptide corresponding to the tyrosine 759 motif of gp130. Taken together, our results suggest differences in the function of SOCS1 and SOCS3 and a link between SHP2 and SOCS3.
Degree
thesis:*- Grantor dc:publisher
- Publikationsserver der RWTH Aachen University
- Year dc:date
- 2001
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Schmitz, Jochen
- Contributors dc:contributor
-
- Heinrich, Peter C.
Subjects
dc:subject × 6Rights
dc:rights- Statement dc:rights
-
- info:eu-repo/semantics/openAccess
- Language dc:language
- ger