Lysine 263 residue of NPM/B23 is essential for regulating ATP binding and B23 stability
نویسندگان
چکیده
منابع مشابه
Disruption of ATP binding destabilizes NPM/B23 and inhibits anti-apoptotic function.
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 a...
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MRP1 (multidrug resistance protein 1) couples ATP binding/hydrolysis at its two non-equivalent NBDs (nucleotide-binding domains) with solute transport. Some of the NBD1 mutants, such as W653C, decreased affinity for ATP at the mutated site, but increased the rate of ATP-dependent solute transport. In contrast, other NBD1 mutants, such as K684L, had decreased ATP binding and rate of solute trans...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2008
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2008.02.059