Charakterisierung der Interaktion von gp130 und Jak1

The subject of this dissertation is the interaction of gp130 and Jak1. Two aspects of this interaction were the main focus: Using FRAP (fluorescence recovery after photobleaching), it was demonstrated that there the kinase Jak1 has the same mobility as gp130 regardless of its kinase activity. This means that there is no constant exchange with a cytoplasmatic pool of Jak1 and there is a constant association of Jak1 and gp130. In the second part of this dissertation, flow-cytometry was used to show that Jak1, Jak2 and Tyk2 have an influence on the surface expression of gp130. Not its kinase activity, but the 3-dimensional structure of Jak1 seems to be responsible for this effect. The upregulation seems to be dependend on internalization, because after mutation of the dileucin-motiv, no upregulation could be observed. This whole mechanism could serve as a quality-control so that only gp130 molecules which have bound Jak1 are on the cell surface to transduct the signals of the ligand.

Grantor dc:publisher

Publikationsserver der RWTH Aachen University

Year dc:date

2007

Author dc:creator

• Diefenbach, Sandra Christiane

Contributors dc:contributor

• Heinrich, Peter C.

• info:eu-repo/classification/ddc/610
• Medizin
• Jak1
• gp130
• Oberflächenexpression
• Hochregulation
• surface-expression
• upregulation

Statement dc:rights

• info:eu-repo/semantics/openAccess

Language dc:language

ger

Identifier

https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-124093%22

OAI identifier oai:identifier

oai:publications.rwth-aachen.de:62529