Investigating the significance of α-interface hot spots on K-Ras homodimer formation

Date

2025-7

Author

Çakır, Bengü İrem

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K-Ras protein, found in the GTPase-binding protein family, is one of the key molecules involved in cell growth and differentiation. It plays a role in transmitting signals from the external environment to the cell nucleus. The KRAS gene is one of the most frequently mutated genes (oncogenes) in human cancers. When mutated, cell undergoes aggressive growth. In recent years, it has been shown that the K-Ras protein can interact with itself and other proteins. Studies have demonstrated that the K-Ras protein can form homo-dimers(K-Ras - K-Ras) and that this dimer structure can affect K-Ras activation and signalling pathways. It has been suggested that alpha-interface of K-Ras protein is particularly important for the formation of homodimers, and specific amino acids at certain positions (hot spots) in this interface can contribute to K-Ras homodimer formation by forming salt bridges. However, the effect of these amino acids which are thought to play a critical role in K-Ras homodimerization has not yet been demonstrated. In this study, the effect of these specific amino acids, located in the K-Ras alpha-interface, on K-Ras homodimer structure was shown using FRET method in live cells.

Subject Keywords

K-Ras, Protein Interactions, Dimerization, α-interface, FRET

URI

https://hdl.handle.net/11511/115477

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Graduate School of Natural and Applied Sciences, Thesis