RNF41 is an E3 ubiquitin-protein ligase that regulates protein degradation through both canonical and noncanonical ubiquitination pathways. The protein demonstrates tissue-specific and context-dependent functions across different cellular processes. In immune regulation, RNF41 controls cytokine receptor trafficking by ubiquitylating and destabilizing USP8, which indirectly affects ESCRT-0 complex stability and determines whether receptors undergo lysosomal degradation or recycling 1. In autophagy regulation, RNF41 activates AMPK/mTOR-mediated autophagy pathways, and its expression is negatively regulated by METTL3/YTHDC1-mediated m6A modifications that shorten mRNA half-life 2. RNF41 exhibits opposing roles in different cancers: it promotes prostate cancer metastasis by stabilizing MYO1C through K27- and K63-linked polyubiquitination, leading to actin remodeling 3, while functioning as a tumor suppressor in bladder cancer by ubiquitinating NUDC to promote its degradation and prevent β-tubulin polymerization 4. In inflammatory skin diseases, RNF41 normally inhibits JAK1-mediated STAT3 activation, but this function is disrupted by KRT6A 5. Genetic variants in RNF41 are associated with congenital heart disease risk 6 and human height variation 7, highlighting its developmental importance.