{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRNF41 (also known as Nrdp1 or NRDP1) is a RING finger‐containing E3 ubiquitin ligase that plays a central role in controlling the abundance and signaling of key receptors. It promotes ligand‐independent ubiquitination and proteasome‐dependent degradation of receptor tyrosine kinases such as ErbB3 and ErbB4—thereby ensuring proper steady‐state receptor levels in normal cells and suppressing aberrant signaling in cancer cells. RNF41 activity is tightly regulated by self‐ubiquitination and interactions with deubiquitinating enzymes (notably USP8), which together modulate its stability and, in turn, influence cytokine receptor trafficking and downstream signaling cascades that control cell growth, apoptosis, and differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in receptor quantity control, RNF41 influences diverse cellular processes by targeting other substrates. It aids in the degradation of apoptosis regulators like BRUCE, thereby modulating cell death in tumors, and it participates in the regulation of receptor recycling versus shedding to fine‐tune signaling responses. In epithelial cells, phosphorylation of RNF41 by kinases such as Par‐1 is required for proper localization of extracellular matrix receptors and for the establishment of apical–basal polarity. RNF41 also regulates kinetochore assembly through the ubiquitination of key mitotic proteins (e.g. SGT1) and has been shown to affect cellular responses to oxidative stress and proliferation, with its expression controlled by mechanisms including oligomerization (via its coiled–coil domain) and microRNAs (such as miR‑497). In addition, RNF41 can interact with viral proteins (for instance, HPV16 E2 and HBx) to impact the stability of receptors involved in oncogenic signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAlterations in RNF41 expression and function have been implicated in a variety of human diseases. Reduced or destabilized RNF41 contributes to oncogenic receptor overexpression in cancers (including breast, glioma, colorectal, hepatocellular, and prostate cancers), facilitating enhanced cell survival, migration, invasion, and metastasis. In contrast, upregulation or stabilization of RNF41 has been associated with improved receptor degradation and pro‑apoptotic effects. Moreover, genetic variants in RNF41 have been linked to congenital heart disease and even traits as complex as human height, while its role in pathways such as TLR4 signaling and in maintaining vascular endothelial integrity suggests broader involvement in inflammatory and metabolic disorders. These findings collectively point to RNF41 as a multi‐faceted regulatory protein whose ubiquitin ligase activity is critical for cellular homeostasis and which represents a promising target for therapeutic intervention."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "25", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Xiuli Wu, Lily Yen, Lisa Irwin, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Amino-terminal dimerization, NRDP1-rhodanese interaction, and inhibited catalytic domain conformation of the ubiquitin-specific protease 8 (USP8)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M606704200"}], "href": "https://doi.org/10.1074/jbc.M606704200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17035239"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17035239"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Xiao-Bo Qiu, Shirley L Markant, Junying Yuan, et al. 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