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USP15 deubiquitinates MDM2. 7 / 8
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"Considering the USP15-MDM2 direct association and the role of USP15 in stabilizing MDM2 and inhibiting MDM2 ubiquitination in activated T cells (XREF_FIG), we examined whether USP15 directly deubiquitinates MDM2."
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"By specifically antagonizing MDM2 auto-ubiquitination, the DUB USP15 prevents NFATc2 dependent gene activation, including IFN-gamma production."
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"USP15 deubiquitylates MDM2, an E3 ligase that ubiquitylates and degrades P53 as well as NFATc2."
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"USP15 deficiency enhances NFATc2 activation in naive CD4 T cells, because USP15 deubiquitinates and stabilizes the E3 ubiquitin ligase MDM2, which negatively regulates NFATc2 activation and cytokine i[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"In melanoma and colorectal cell lines, deletion of USP15 induces MDM2 auto-ubiquitination and degradation and USP15 negatively regulates the T-cell transcription factor NFATc2 by decreasing MDM2 auto-ubiquitination and degradation, thereby inhibiting T-cell proliferation and activation (Fig. 2C).35However, MDM2 inhibits T cell apoptosis and promotes T cell proliferation and activation."
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"Under normal condition, a DUB, Usp15, deubiquitinates MDM2 to inhibit MDM2 degradation, thereby negatively regulating the generation of IFN-gamma-producing Th1 effector T cells."
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"Murine double minute 2 (MDM2), a well-known negative modulator of p53 [71], can be deubiquitinated by USP15 to degrade nuclear factor of activated T cells c2 (NFATc2), which is crucial for T-cell-related cytokine (e.g., IL-2 and IFN-γ) expression (Fig. 2)."
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