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Abstract
The c‑Myc oncoprotein is frequently dysregulated in human cancers, and its functional regulation and degradation are critical targets for therapeutic intervention. This study uses Saccharomyces cerevisiae as a model system to investigate c‑Myc phosphorylation, stability, and protein interactions. c‑Myc was shown to undergo sequential, interdependent phosphorylation at threonine 58 and serine 62 in yeast, mirroring regulation observed in mammalian cells and affecting protein stability. Yeast orthologs of known mammalian regulatory proteins similarly influenced these phosphorylation events, validating yeast as a relevant model. A yeast two‑hybrid screen identified ten novel c‑Myc interacting proteins, including HBP1, a tumor suppressor. HBP1 was found to bind c‑Myc and inhibit its transcriptional activity, providing new insight into c‑Myc regulation and tumor suppression.