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E3 ubiquitin-protein ligase NRDP1 (RNF41) is an enzyme that catalyzes the transfer of ubiquitin to specific target proteins, marking them for proteasomal or lysosomal degradation[1][3][4]. It contains a RING finger domain that mediates protein-protein interactions necessary for ubiquitin transfer[1][5]. RNF41 regulates the stability and turnover of several cytokine and growth factor receptors, including erythropoietin receptor, interleukin-3 receptor, and ErbB3[2][3]. It negatively modulates pro-inflammatory signaling (such as MyD88-dependent cytokine production) and plays roles in apoptosis and autophagy/mitophagy by targeting specific signaling molecules for ubiquitination and degradation[3][4][5]. Dysregulation or mutation of RNF41 is implicated in the pathogenesis of cancer, neurodegenerative, autoimmune, and infectious diseases[4][5]. RNF41 interacts with various cellular proteins, including USP8, BRUCE, Parkin (PRKN), VPS52, and participates in dynamic subcellular protein sorting[2].
Ubiquitination-dependent degradation (mainly K48-linked polyubiquitination), Negative regulation of receptor signaling via polyubiquitination and subsequent proteasomal or lysosomal degradation
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