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

David Schwefel

doi:10.1016/j.str.2023.10.004

Cullin(g) glutamate dehydrogenase: Insights into multivalent CRL3^KLHL22 substrate recognition

Structure. 2023 Nov 2;31(11):1294-1296. doi: 10.1016/j.str.2023.10.004.

Author

David Schwefel¹

Affiliation

¹ Technische Universität Berlin, Chair of Bioanalytics, 10623 Berlin, Germany. Electronic address: schwefel@tu-berlin.de.

PMID: 37922866
DOI: 10.1016/j.str.2023.10.004

Abstract

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 CRL3^KLHL22 E3 ligase assembly with a hexameric substrate and its possible implications for metabolic adaptation and oncogenesis.

MeSH terms

Cullin Proteins* / metabolism
Glutamate Dehydrogenase* / metabolism
Ubiquitin-Protein Ligases / metabolism
Ubiquitination

Substances

Cullin Proteins
Glutamate Dehydrogenase
Ubiquitin-Protein Ligases