Structural mimicry of UM171 and neomorphic cancer mutants co-opts E3 ligase KBTBD4 for HDAC1/2 recruitment - Chen, Zhuoyao; Chi, Gamma; Balo, Timea; Chen, Xiangrong; Montes, Beatriz Ralsi; Clifford, Steven C.; D’Angiolella, Vincenzo; Szabo, Timea; Kiss, Arpad; Novak, Tibor; Herner, András; Kotschy, András; et al. (Nature communications, 2025)
Keywords: 101/28; 13/1; 13/106; 13/109; 13/44; 14/1; 631/45/474/2073; 631/45/535/1258/1259; 631/67/395; 631/80/304; 631/92/613; 82/16; 82/29; 82/58; 82/80; 9/10; Cancer; Co-Repressor Proteins - genetics; Co-Repressor Proteins - metabolism; Cryoelectron Microscopy; Epigenetics; HDAC2 protein; Hematopoietic stem cells; Histone deacetylase; Histone Deacetylase 1 - chemistry; Histone Deacetylase 1 - genetics; Histone Deacetylase 1 - metabolism; Histone Deacetylase 2 - chemistry; Histone Deacetylase 2 - genetics; Histone Deacetylase 2 - metabolism; Humanities and Social Sciences; Humans; Immunosuppressive agents; Medulloblastoma; Mimicry; Mode of action; multidisciplinary; Mutants; Mutation; Protein Binding; Science; Science (multidisciplinary); Stem cell transplantation; Stem cells; Ubiquitin-protein ligase; Ubiquitin-Protein Ligases - chemistry; Ubiquitin-Protein Ligases - genetics; Ubiquitin-Protein Ligases - metabolism; Ubiquitination