Ontology highlight
ABSTRACT:
SUBMITTER: Horn-Ghetko D
PROVIDER: S-EPMC7904520 | biostudies-literature | 2021 Feb
REPOSITORIES: biostudies-literature
Horn-Ghetko Daniel D Krist David T DT Prabu J Rajan JR Baek Kheewoong K Mulder Monique P C MPC Klügel Maren M Scott Daniel C DC Ovaa Huib H Kleiger Gary G Schulman Brenda A BA
Nature 20210203 7847
E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates<sup>1,2</sup>. However, rather than functioning individually, many neddylated cullin-RING E3 ligases (CRLs) and RBR-type E3 ligases in the ARIH family-which together account for nearly half of all ubiquitin ligases in humans-form E3-E3 super-assemblies<sup>3-7</sup>. Here, by studying CRLs in the SKP1-CUL1-F-box (SCF) ...[more]