IndraLab

Statements

USP15 activates MDM2. 7 / 10
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"We found that USP15 mediates the stability of MDM2 in both T cells and cancer cells."
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"Because of the ubiquitin dependent degradation, together with TCR and CD28 stimulation, MDM2 can be transiently down-regulated, and the loss of USP15 greatly promotes the degradation of MDM2 in T cells."
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"We next examined whether USP15 directly targets MDM2."
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"These results suggest that USP15 prevents the ubiquitin dependent degradation of MDM2 in activated T cells."
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"Notably, USP15 enhances the protein stability of MDM2, which subsequently inhibits T cell activation by facilitating the degradation of the transcription factor NFATc2, thereby suppressing anti-tumor T cell responses (Zou et al., 2014)."
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"In both activated T cells and cancer cells, loss of USP15 caused MDM2 degradation."
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"The expression of TIFAB in HSCs allows the signaling of USP15 to different substrates, including MDM2 and KEAP1, leading to a decrease in TP53 expression, which may consequently promote leukemic transformation."
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