RGD Reference Report - Disruption of ATP binding destabilizes NPM/B23 and inhibits anti-apoptotic function. - Rat Genome Database

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Disruption of ATP binding destabilizes NPM/B23 and inhibits anti-apoptotic function.

Authors: Choi, JW  Lee, SB  Ahn, JY  Lee, KH 
Citation: Choi JW, etal., BMB Rep. 2008 Dec 31;41(12):840-5.
RGD ID: 11534995
Pubmed: PMID:19123973   (View Abstract at PubMed)

Nucleophosmin/B23, a major nucleolar phosphoprotein, is overexpressed in actively proliferating cells. In this study, we demonstrate that B23 exclusively localizes in the nucleolus, whereas ATP depletion results in the redistribution of B23 throughout the whole nucleus and destabilizes B23 via caspase-3 mediated cleavage. Interestingly, ATP binding precedes PI(3,4,5)P(3) binding at lysine 263 and ATP binding mutants fail to restore the anti-apoptotic functions of B23 in PC12 cells. Thus, the ATP-B23 interaction is required for the stability of the B23 protein and regulates cell survival, confining B23 within the nucleolus in PC12 cells.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
negative regulation of neuron apoptotic process  IMP 11534995 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
ATP binding  IMP 11534995 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Npm1  (nucleophosmin 1)


Additional Information