IndraLab

Statements

AKT phosphorylates NPM1 on S48. 11 / 11
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"The data presented above argues that phosphorylation of NPM-Ser48 by AKT promotes the nucleoplasmic localization of ARF."
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"We find that AKT phosphorylation of NPM-Ser48 prevents oligomerization that results in nucleoplasmic localization of ARF, constitutive MDM2 inhibition and stabilization of p53."
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"Phosphorylated NPM, but not a NPM-S48A derivative, can be detected with a specific phospho-peptide antibody (pS48-NPM) (Fig. xref and xref ) and furthermore, NPM-Ser48 could be phosphorylated by AKT in response to EGF stimulation ( xref )."
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"The NPM/ARF interaction can be disrupted by DNA damage as well as phosphorylation of NPM at Ser48 by Akt, both of which lead to ARF’s nucleoplasmic transition and interaction with MDM2. xref , xref Following DNA damage, cJun can interact with NPM and cause NPM and ARF redistribution, an event that requires JunB, JNK activation and its phosphorylation of cJun at Thr91 and Thr93. xref "
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"Moreover, site directed mutants of NPM that restrict oligomerization also perturb ARF association and nucleolar targeting [ xref , xref , xref ], suggesting that phosphorylation of NPM-Ser48 by AKT may also impact ARF localization and stability."
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"We confirmed that AKT specifically phosphorylated NPM on Ser48 by in-vitro kinase assay."
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"We find that AKT phosphorylation of NPM-Ser48 inhibits NPM oligomerisation and localization at the nucleolus."
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"AKT phosphorylation of NPM-Ser48 regulates NPM oligomerization."
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"Taken together these results suggest that nucleolar localization of both ARF and NPM are disrupted by AKT phosphorylation of NPM-Ser48, but that a stable pool of NPM persists in oligomeric form."
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"We confirmed that AKT specifically phosphorylated NPM on Ser48 by in-vitro kinase assay (Fig. xref )."
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"Having established that the phosphorylation of NPM-Ser48 by AKT promotes ARF nucleoplasmic localization, MDM2 inhibition and the stabilization of p53 mut , we next wished to address if phosphorylation of NPM-Ser48 was a common phenomenon, and potentially contributing to the stabilization of p53 mut in human tumors."
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