DCAF7 is a WD40-repeat protein that functions as a substrate recognition receptor for the CUL4-DDB1 E3 ubiquitin ligase complex, regulating protein stability across multiple cellular processes. In development, DCAF7 acts upstream of the EDN1 signaling pathway and associates with DYRK1A and DIAPH1 to control GLI1 transcriptional activity and craniofacial morphogenesis. In DNA replication and repair, DCAF7 maintains appropriate levels of DNA ligase I and the ERCC1-XPF nucleotide excision repair complex, with DCAF7 depletion impairing UV-induced damage repair 12. In cancer contexts, DCAF7 promotes aggressive phenotypes through distinct mechanisms. In nasopharyngeal carcinoma, DCAF7 serves as a scaffold recruiting the deubiquitinase USP10 to stabilize G3BP1, enhancing stress granule formation and conferring cisplatin resistance 3. In pancreatic neuroendocrine tumors, DCAF7-mediated ubiquitination of the MEN1 tumor suppressor promotes its degradation; DCAF7 downregulation sensitizes everolimus-resistant tumors to mTOR inhibition 4. In hepatocellular carcinoma, DCAF7 recruits USP2 to suppress ferroptosis by preventing clockophagy-induced degradation of the circadian regulator BMAL1 5. DCAF7 is also an antiviral restriction factor; it targets the influenza A viral polymerase PA subunit for degradation via CRL4B-mediated ubiquitination 6. Additionally, DCAF7 regulates myogenic transcription by stabilizing DYRK1A in a complex that phosphorylates RNA polymerase II 7, and emerging evidence identifies DCAF7 as a potential candidate gene in neurodevelopmental disorders 8.