Thesis supervisor: Beáta Albert
Location of studies (in Hungarian): Csíkszereda Abbreviation of location of studies: Csík
Description of the research topic:
Recent research has revealed that the programmed cell death is not only done by apoptosis, but also by programmed necrosis as well. In the regulation of apoptosis-necrosis response the protein family of RIP (receptor interacting serine threonine kinase) has a pivotal role, which mediates cell death in the direction of apoptosis or necroptosis through a RIPoptosome complex.
The RIPoptosome is regulated by XIAP and CIAP proteins (RIP1, FADD, pro- caspase 8) by ubiq-uitination of the components, so inhibiting it and forcing the cells towards apoptosis on the caspase-dependent pathway. However, if the ubiquitonation of RIP1 is inhibited, it activates another complex, the FADD and the caspase 8 and forcing the cell to enter necroptosis. In some cells caspase 10 is involved. It is unclear whether it is necessary the autophosphorylation of the RIP for the assembly of the RIPoptosome. In the next step the RIP1 phosphorylates the RIP3 kinase, which forces the cell to enter in caspase independent necroptosis through free radical production.
The clarification of the cross-talk between CIAP, RIP1, RIP3 and more caspases could reveal that the cell depending on the post-translational modifications of these molecules (ubiquitinations and phosphorylations) in which type of cell death (necroptosis or apoptosis) enters.
Our goal is to clarify the post-translational modifications in experiments using the wild and mutant forms of the protein. By measuring the components interactions we can have a better understand-ing of the complex operation.
Number of students who can be accepted: 1
Deadline for application: 2017-12-02
2024. IV. 17. ODT ülés Az ODT következő ülésére 2024. június 14-én, pénteken 10.00 órakor kerül sor a Semmelweis Egyetem Szenátusi termében (Bp. Üllői út 26. I. emelet).
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