Publikationsserver der RWTH Aachen University
Analyse der Dimerisierung des Zytokin-Rezeptors gp130 mit Hilfe von YFP-IL-6, einem funktionellen Fusionsprotein aus Interleukin-6 und dem yellow fluorescent protein
Abstract
dc:descriptionCytokines are important mediators of intercellular communication in higher organisms. The subfamily of haematopoietic cytokines plays a central role in the regulation of haematopoiesis and the immune response. From knockout studies, it became evident that these mediators are also involved in the regulation of other fundamental biological processes such as embryonic development (Yoshida et al., 1996) and fertility (Robb et al., 1998; Stewart et al., 1992). The cytokine receptor gp130 is the shared signalling subunit of the IL-6-type cytokines. Interleukin-6 (IL-6) signals through gp130 homodimers Related haematopoietic receptors such as the erythropoietin receptor have been described as preformed dimers in the plasma membrane. In this work we investigated gp130 homodimerization by using a fluorescent fusion protein of IL-6 and YFP (YFP-IL-6). We observed that the simultaneous action of two IL-6 binding domains on two gp130 molecules is required to efficiently recruit a fluorescent IL-6 (YFP-IL-6) to the plasma membrane. These data were supported by the observation that a a FRET signal could been detected between YFP- and CFP-tagged gp130 at the plasma membrane of unstimulated cells that does not increase upon IL-6 stimulation. Taken together, these findings suggest that transient gp130 homodimers on the plasma membrane are stabilized by IL-6.
Degree
thesis:*- Grantor dc:publisher
- Publikationsserver der RWTH Aachen University
- Year dc:date
- 2008
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Roderburg, Christoph
- Contributors dc:contributor
-
- Müller-Newen, Gerhard
Subjects
dc:subject × 14Rights
dc:rights- Statement dc:rights
-
- info:eu-repo/semantics/openAccess
- Language dc:language
- ger