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SP1 binds BAP1. 16 / 16
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"Therefore, ODN enhanced oxaliplatin-induced apoptosis by interacting with BAP1 and Sp1 to induce Sp1 stabilization-mediated Bax upregulation ( xref )."
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"ODN induces BAP1 interaction with Sp1."
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"We postulated that ODN may influence the interaction between BAP1 and Sp1."
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"Interestingly, ODN and cathepsin K siRNA treatment markedly increased Sp1 and BAP1 interaction ( xref A)."
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"Sp1-BAP1 interaction was increased by ODN treatment ( xref F)."
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"ODN induced the phosphorylation of BAP1 at Ser 592 and enhanced the interaction of Sp1 and BAP1, resulting in Sp1 deubiquitination and destabilization."
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"We postulated that ODN may influence the interaction between BAP1 and Sp1."
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"Mechanistically, ODN induced BAP1 phosphorylation and enhanced Sp1-BAP1 interaction, resulting in Sp1 ubiquitination and degradation."
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"To investigate the functional role of p53, we tested the interaction between Sp1 and BAP1 after p53 immunoprecipitation in ODN- and cathepsin K siRNA-treated cells and identified more p53, Sp1, and BAP1 protein complexes in the ODN- and cathepsin K siRNA-treated cells ( xref B)."
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"These data demonstrated that the C-terminal domain of p53 can effectively enhance Sp1 stability by increasing the interaction with BAP1 and Sp1."
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No evidence text available
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"To verify the interaction with BAP1 and Sp1, we performed the proximity ligation assay."
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"Interestingly, ODN and cathepsin K siRNA treatment markedly increased Sp1 and BAP1 interaction (Fig. 7A)."
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"To investigate the functional role of p53, we tested the interaction between Sp1 and BAP1 after p53 immunoprecipitation in ODN- and cathepsin K siRNA-treated cells and identified more p53, Sp1, and BAP1 protein complexes in the ODN- and cathepsin K siRNA-treated cells (Fig. 7B)."
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No evidence text available
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"ODN induced the phosphorylation of BAP1 at Ser 592 and enhanced the interaction of Sp1 and BAP1, resulting in Sp1 deubiquitination and destabilization."
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