Ceejay Lee

Feb 12, 2025 | nature.com | Xiaowen Xie |Olivia Zhang |Ceejay Lee |N. Connor Payne |Leena Paul |Yiran Li | +10 more

AbstractCancer mutations can create neomorphic protein–protein interactions to drive aberrant function1,2. As a substrate receptor of the CULLIN3-RING E3 ubiquitin ligase complex, KBTBD4 is recurrently mutated in medulloblastoma3, the most common embryonal brain tumour in children4. These mutations impart gain-of-function to KBTBD4 to induce aberrant degradation of the transcriptional corepressor CoREST5. However, their mechanism remains unresolved.