IndraLab

Statements


CK2 phosphorylates NPM1 on S125. 7 / 9
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reach
"In addition, B23 can be phosphorylated at serine 125 by casein kinase II (CKII), and this phosphorylation is restricted to interphase [20] ."

sparser
"The study demonstrated that CIGB-300 inhibited CK2-dependent phosphorylation of NPM1 at S125 and induced nucleolar disorganization."

sparser
"CK2 phosphorylates NPM at Ser125, which is located in one of NPM’s acidic stretches, a region that, along with its N-terminal oligomerization domain, is essential for its chaperone activity. xref Thus, CK2 phosphorylation promotes the dissociation of substrates bound to NPM. xref Furthermore, this phosphorylation during interphase enhances NPM movement through the nucleolus. xref NPM is necessary not only for pre-rRNA processing, but for the transport and nuclear export of both 40S and 60S ribosomal subunits. xref , xref , xref CK2, along with CDK1, phosphorylation may help reduce NPM’s nucleolar localization during mitosis and interfere with its binding to rRNA or ribosomal components, thereby inhibiting ribosome biogenesis."

sparser
"CK2 phosphorylation of NPM1 at S125 is important for the nucleolar organization ( xref )."

reach
"CK2 phosphorylates NPM at Ser125, which is located in one of NPM 's acidic stretches, a region that, along with its N-terminal oligomerization domain, is essential for its chaperone activity."

reach
"CK2 phosphorylation of NPM1 at S125 is important for the nucleolar organization (114)."

reach
"The study demonstrated that CIGB-300 inhibited CK2-dependent phosphorylation of NPM1 at S125 and induced nucleolar disorganization."