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Ring finger protein 11 (RNF11) is a small, 154-amino-acid protein containing a canonical RING-H2 finger motif critical for mediating protein-protein interactions and E3 ubiquitin ligase activity.[1][2][3] RNF11 acts as a regulator and modulator of other E3 ligases, especially the NEDD4 family of HECT-type ligases, influencing substrate selection and stability through ubiquitin-mediated degradation. This makes RNF11 a central player in diverse signaling pathways, including TGF-β, NF-κB, and EGFR, thereby controlling processes such as inflammation, cell growth, and endosomal sorting. It is implicated in diseases like cancer and neurodegenerative disorders, where its overexpression or dysregulation alters key cellular processes.[1][2][3]
Not established for direct targeting, but mechanistic roles for modulation include: Inhibition of ubiquitin ligase activity; Blocking protein-protein interactions within E3 ligase complexes; Modulation of downstream signaling pathways (e.g., NF-κB, TGF-β).
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