作者: Vanessa Lopez-Pajares , Mihee M. Kim , Zhi-Min Yuan
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摘要: The critical tumor suppressor p53 is mutated or functionally inactivated in nearly all cancers. We have shown previously that the MDM2-MDMX complex functions as an integral unit targeting for degradation. Here we identify small protein 14-3-3 a binding partner of MDMX, which binds at C terminus (Ser367) phosphorylation-dependent manner. Importantly, demonstrate serine/threonine kinase Akt mediates phosphorylation MDMX Ser367. This leads to stabilization and consequent MDM2. Previous studies phosphorylates stabilizes Our data suggest by may be alternative mechanism up-regulates MDM2 levels exerts its oncogenic effects on cells.