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RNF187 is a RING-type E3 ubiquitin ligase enzyme that facilitates the transfer of ubiquitin from E2 enzymes to substrate proteins, thereby influencing their degradation, activity, or cellular localization. It functions as a coactivator for JUN-mediated gene activation in response to growth factor signaling (via the MAP3K1 pathway) and is directly involved in protein ubiquitination. RNF187 is localized in both the cytosol and nucleoplasm. Biologically, RNF187 is implicated as a modulator of P53 signaling in breast cancer, promoting tumor growth and inhibiting apoptosis through P53 polyubiquitination and degradation independently of MDM2. Its dysregulation is associated with poor cancer prognosis, and it may serve as a novel cancer therapeutic target. Broader relevance exists for the RING family of E3 ligases in neurodevelopmental and congenital disorders. If more detailed information on interacting drugs becomes available, it can be appended, but currently, there are no FDA-approved drugs directly targeting RNF187.
Modulation of substrate ubiquitination. Promotion of polyubiquitination and degradation of P53, impacting apoptosis and cell growth (mechanism described for experimental inhibitors/modulators but no direct drugs listed).
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