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ABSTRACT:
SUBMITTER: Kostrhon S
PROVIDER: S-EPMC8460447 | biostudies-literature | 2021 Oct
REPOSITORIES: biostudies-literature
Kostrhon Sebastian S Prabu J Rajan JR Baek Kheewoong K Horn-Ghetko Daniel D von Gronau Susanne S Klügel Maren M Basquin Jérôme J Alpi Arno F AF Schulman Brenda A BA
Nature chemical biology 20210913 10
An emerging mechanism of ubiquitylation involves partnering of two distinct E3 ligases. In the best-characterized E3-E3 pathways, ARIH-family RING-between-RING (RBR) E3s ligate ubiquitin to substrates of neddylated cullin-RING E3s. The E3 ARIH2 has been implicated in ubiquitylation of substrates of neddylated CUL5-RBX2-based E3s, including APOBEC3-family substrates of the host E3 hijacked by HIV-1 virion infectivity factor (Vif). However, the structural mechanisms remained elusive. Here structur ...[more]