IndraLab

Statements


NPM1 is phosphorylated on S48. 9 / 9
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sparser
"These results suggest that AKT mediated phosphorylation of NPM-Ser48 promotes cellular resistance to IR by promoting ARF relocalization to the nucleoplasm and the stabilization of p53 mut ."

sparser
"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."

sparser
"In the presence of myr-AKT1, we observed an increased monomeric NPM fraction, corresponding with increased NPM-S48 phosphorylation, implying that phosphorylation prevents NPM oligomers in a Ser48 dependent manner (Fig. xref , lanes 4-6)."

rlimsp
"Besides, AKT-mediated phosphorylation of NPM-Ser48 can prevent the oligomerization of NPM1, and subsequently results in nucleoplasmic localization of p14ARF, constitutive HDM2 inhibition and stabilization of p53."

sparser
"It has been reported that ATM-mediated phosphorylation of NPM1 can inhibit the binding of NPM1 with p14ARF, and thereby promoting the translocation of p14ARF to nucleoplasm. xref , xref Besides, AKT-mediated phosphorylation of NPM-Ser48 can prevent the oligomerization of NPM1, and subsequently results in nucleoplasmic localization of p14ARF, constitutive HDM2 inhibition and stabilization of p53. xref However, we observed no effect of SOX6 on the phosphorylation of NPM1."

sparser
"In T24 cells, where NPM is phosphorylated on Ser48 (Fig. xref ), inhibition of AKT decreases the monomeric fraction of NPM ( xref ) and increases NPM oligomers ( xref )."

sparser
"AKT interacts with NPM, resulting in NPM phosphorylation at serine 48 (located in the oligomerization domain)."

sparser
"This suggests that phosphorylation of NPM-Ser48 is a physiological signal that directs NPM localization via the regulation of NPM oligomerisation."

sparser
"Since phosphorylation of NPM-Ser48 appears to dictate both NPM oligomerisation and localization, we wished to address whether this mechanism may also affect NPM interacting proteins that are functionally controlled by trafficking to and from the nucleolus [ xref ]."