Phosphorylation Code of Human Nucleophosmin Includes Four Cryptic Sites for Hierarchical Binding of 14-3-3 Proteins

• Published in: Journal of molecular biology Vol. 436; no. 12; p. 168592
• Main Authors: Kapitonova, Anna A., Perfilova, Kristina V., Cooley, Richard B., Sluchanko, Nikolai N.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Ltd 15.06.2024
• Subjects: 14-3-3 Proteins - chemistry; 14-3-3 Proteins - genetics; 14-3-3 Proteins - metabolism; Binding Sites; cryptic disorder; domain-motif interaction; fluorescence anisotropy; Humans; Nucleophosmin - chemistry; Nucleophosmin - genetics; Nucleophosmin - metabolism; oligomeric state transition; Phosphorylation; Protein Binding; Protein Multimerization; cryptic disorder; domain-motif interaction; oligomeric state transition; phosphorylation; fluorescence anisotropy

[Display omitted] •NPM1 is phosphorylated by PKA at multiple sites phosphorylatable in vivo.•Phosphorylation drives NPM1 unfolding, monomerization and recruits 14-3-3.•Four NPM1 phosphoserines are recognized by all seven human 14-3-3 isoforms.•Binding of phosphomotifs is hierarchical, pS293 > pS4...