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Abstract
Protein Phosphatase 2A (PP2A) is a major cellular phosphatase with tumor suppressor functions, primarily through dephosphorylation of c-MYC at Serine62. Phosphorylation at this site stabilizes c-MYC and promotes oncogenesis, yet mechanisms of PP2A deregulation in cancer remain unclear. This thesis investigates how PP2A activity is suppressed by oncoprotein overexpression and explores strategies to reactivate PP2A, aiming to restore normal signaling and modulate c-MYC-driven pathways.