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Updated: Jun 26, 2026

Characterization of MLKL-mediated Plasma Membrane Rupture in Necroptosis
Published on: August 7, 2018
Disruption of ATP binding destabilizes NPM/B23 and inhibits anti-apoptotic function
Joung Woo Choi1, Sang Bae Lee, Jee-Yin Ahn
1Department of Anatomy, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
Abstract:
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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