Kovalente und nicht-kovalente Interaktion ligandengesteuerter Ionenkanäle mit Ubiquitin in Xenopus-laevis-Oozyten

This thesis dealt with the possibility of modification of cys-loop-receptors by ubiquitination, especially the Glycine-receptor and GABA-receptor. Ubiquitin is a small intracellular protein, which marks other cellular proteins for proteolytic degradation by the proteasome on the one hand and for endocytic elimination from the plasma membrane on the other hand. In this context the theory of the E3-ligase Parkin mediating ubiquitination was examined but could not be proved. Blue-native-PAGE-analysis showed that the GABAA-a1-subunits assemble as homotrimers and not as pentamers what is known of cys-loop-receptors. Coexpression of GABAA-a1 and GABAA-b2-subunits showed the typical pentamer assembly. In contrast to this Glyince-alpha1-subunits showed their ability to assemble in pentamers. Moreover the formation of a covalent adduct between the alpha1-subunit of the Glycine-receptor and GST-ubiquitin which was dependant on lysines of the intracellular loop of the alpha1-subunit could be demonstrated in this thesis.

Grantor dc:publisher

Publikationsserver der RWTH Aachen University

Year dc:date

2006

Author dc:creator

• Chakravertty, Anastasia

Contributors dc:contributor

• Schmalzing, Günther

• info:eu-repo/classification/ddc/610
• Medizin
• Ionenkanal
• Ubiquitin
• Ubiquitin-Protein-Ligase
• GABA-Rezeptor
• Glycin
• Glatter Krallenfrosch
• Glycin-Rezeptor
• Parkin
• Synphilin
• SDS-PAGE
• BN-PAGE

Statement dc:rights

• info:eu-repo/semantics/openAccess

Language dc:language

ger

Identifier

https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114745%22

OAI record oai:identifier

https://publications.rwth-aachen.de/oai2d?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Apublications.rwth-aachen.de%3A52529