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

Joung Woo Choi | Zendy; Sang Bae Lee | Zendy; JeeYin Ahn | Zendy; Kyung-Hoon Lee | Zendy

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

Author(s) -

Joung Woo Choi,

Sang Bae Lee,

JeeYin Ahn,

Kyung-Hoon Lee

Publication year - 2008

Publication title -

bmb reports

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.511

H-Index - 77

eISSN - 1976-670X

pISSN - 1976-6696

DOI - 10.5483/bmbrep.2008.41.12.840

Subject(s) - nucleolus , microbiology and biotechnology , nucleophosmin , phosphoprotein , apoptosis , cleavage (geology) , chemistry , nucleus , biology , phosphorylation , biochemistry , paleontology , fracture (geology) , gene

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.

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