DCAF10 (DDB1 and CUL4 associated factor 10) functions as a substrate receptor for the CUL4-DDB1 E3 ubiquitin-protein ligase complex 1, directing the proteasomal degradation of specific target proteins. DCAF10 recognizes N-terminally acetylated substrates, including Src-family kinases (SFKs), where it monitors the replacement of myristoylation by acetylation and triggers ubiquitin-mediated degradation upon detecting this modification 1. The CUL4A-DDB1-DCAF10 complex also targets ALOX15B for degradation in pancreatic cancer contexts, where disruption of this interaction restores ferroptosis sensitivity 2, and promotes MCL1 degradation to activate caspase-dependent apoptosis in esophageal cancer 3. DCAF10 is frequently lost at the genomic level in lung adenocarcinomas 4, suggesting tumor suppressive properties. Additionally, adenovirus E1A exploits DCAF10-containing E3 ligase complexes to degrade RUVBL1/2 AAA+ ATPases, thereby inhibiting interferon responses and promoting viral replication 5. DCAF10 participates in regulating apoptosis and cellular stress responses, with dysregulation implicated in cancer development and chemoresistance.