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. 2020 Jan 1;10(2):797–815. doi: 10.7150/thno.38483

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14-3-3ζ dimer specifically interacts with histone H3 in nucleus. (A) 14-3-3ζ interaction with histone H3 was specially inhibited by PTA. Co-IP was performed with anti-HA antibody followed by silver staining and LC-MS/MS analysis for specific protein bands. HEK293T cells transfected with HA-tagged 14-3-3ζ vector were treated with 20 μM PTA or vehicle. (B) 14-3-3ζ interaction with histone H3 was inhibited by PTA in HA-tagged 14-3-3ζ-transfected HEK293T and Neuro-2A cells. (C) Recombinant 14-3-3ζ protein interaction with recombinant histone H3 protein was inhibited by PTA. (D and E) Cytoplasmic translocation of 14-3-3ζ from nucleus was promoted by PTA. HA-tagged 14-3-3ζ was shown in green, and histone H3 was shown in red (scale bars = 25 μm). (F) 14-3-3ζ dimerization was promoted by PTA in cytoplasm (BiFC, scale bars = 10 μm). (G) Phosphorylation levels of 14-3-3ζ (S58) were increased by PTA.