Lysine 263 residue of NPM/B23 is essential for regulating ATP binding and B23 stability | Zendy

Choi Joung Woo | Zendy; Lee Sang Bae | Zendy; Kim Chung Kwon | Zendy; Lee Kyung-Hoon | Zendy; Cho Sung-Woo | Zendy; Ahn Jee-Yin | Zendy

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Lysine 263 residue of NPM/B23 is essential for regulating ATP binding and B23 stability

Author(s) -

Choi Joung Woo,

Lee Sang Bae,

Kim Chung Kwon,

Lee Kyung-Hoon,

Cho Sung-Woo,

Ahn Jee-Yin

Publication year - 2008

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2008.02.059

Subject(s) - lysine , nucleolus , mutant , binding site , asparagine , chemistry , biochemistry , mutagenesis , microbiology and biotechnology , biology , enzyme , amino acid , cytoplasm , gene

Here, we show that Nucleophsomin/B23 provides lysine 263 as a critical binding site for ATP. Mutagenesis of lysine 263 to asparagine (K263N) disrupts B23 from ATP binding. While B23 WT exclusively localizes to the nucleolus, the B23‐K263N is redistributed from the nucleolus to the nucleoplam. Notably, the K263N mutant is unstable, and displayed rapid degradation. Alteration of K263 induced B23 instability through increased ubiquitination and proteaosomal degradation. Moreover, mutation of K263 impedes the mitogenic effect of B23 in PC12 cells. Thus, K263 is a critical site for ATP binding and required for B23 stability, confining B23 in the nucleolus.

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