RBMS3 is an RNA-binding protein that binds poly(A) and poly(U) oligoribonucleotides 1 and plays multifaceted roles in gene regulation and disease pathogenesis. Mechanistically, RBMS3 regulates mRNA stability and protein expression through 3'UTR binding 2 and can facilitate ubiquitination-mediated protein degradation in an RNA-independent manner 3. RBMS3 acts as a regulator of epithelial-mesenchymal transition and influences Wnt/β-catenin signaling, with its absence activating this pathway 4. In cancer biology, RBMS3 exhibits context-dependent roles. RBMS3 induction suppresses vasculogenic mimicry in glioblastoma by promoting circHECTD1-encoded peptide formation, which drives NR2F1 degradation 1. Conversely, RBMS3 loss drives sorafenib resistance in hepatocellular carcinoma by preventing TRIM21-mediated ANGPT2 ubiquitination, promoting angiogenesis 3. RBMS3 also stabilizes PD-L1 mRNA in triple-negative breast cancer, supporting immune evasion; RBMS3 depletion enhances immunotherapy efficacy 2. Beyond cancer, RBMS3 variants associate with exfoliation syndrome, an age-related extracellular matrix disorder causing glaucoma 5, and interact with ZNF516 to influence bone mineral density in osteoporosis 6. RBMS3 emerges as a diagnostic biomarker for postmenopausal osteoporosis 7. These findings position RBMS3 as a critical post-transcriptional regulator with therapeutic potential across multiple disease contexts.