Cullin(g) glutamate dehydrogenase: Insights into multivalent CRL3KLHL22 substrate recognition

Substrate specificity is central to the regulation of cellular ubiquitylation. In this issue of Structure, Teng et al. employ biochemistry and cryo-EM single-particle reconstruction to clarify the intricate interaction of the dimeric CRL3KLHL22 E3 ligase assembly with a hexameric substrate and its possible implications for metabolic adaptation and oncogenesis. Substrate specificity is central to the regulation of cellular ubiquitylation. In this issue of Structure, Teng et al. employ biochemistry and cryo-EM single-particle reconstruction to clarify the intricate interaction of the dimeric CRL3KLHL22 E3 ligase assembly with a hexameric substrate and its possible implications for metabolic adaptation and oncogenesis. Cryo-EM structure of the KLHL22 E3 ligase bound to an oligomeric metabolic enzymeTeng et al.StructureOctober 2, 2023In BriefKelch-like protein 22 is one of the adapter-substrate receptors of CULLIN3 ubiquitin ligase. Teng et al. report the cryo-EM structure of KLHL22 E3 ligase that dynamically associates with GDH1 and mediates its polyubiquitination. These findings shed light on the architectural details of this E3 ligase during ubiquitination. Full-Text PDF