THE ROLE OF G-DOMAIN ON K-RAS AND Gα DIMERIZATION

Date

2024-1-26

Author

Aydın, İrem

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K-Ras protein is a member of the Ras superfamily, also known as a small G protein, and plays roles in different signaling pathways via binding and activating various effectors. Most of these pathways enable cellular activities such as cell proliferation, migration, survival, and differentiation. The G-domain, which is common to all G-proteins, is defined as the active site of these proteins. Some of the mutations in this domain affect protein function and protein-protein interactions. These mutations, which cause the K-Ras protein to remain constitutively active, have been detected in many types of cancer by various research groups. Studies in recent years have shown that proteins belonging to the Ras family form dimers, which play essential roles in numerous signaling pathways. In this study, the physical interactions between K-Ras and Gα proteins and the regions that have been identified as hot spots in K-Ras homodimerization, which are also conserved in Gα proteins, has been exposed to site-directed mutagenesis and the impact of these conserved regions on the possible K-Ras - Gα heterodimerization has been investigated using FRET technique.

Subject Keywords

K-Ras, Gα Proteins, Protein Interactions, Dimerization, FRET

URI

https://hdl.handle.net/11511/108458

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Graduate School of Natural and Applied Sciences, Thesis