Here, our structures and biochemistry reveal distinctive autoinhibition and activation
mechanisms of the ARIH RBR E3 ligase ARIH2. It is activated upon super-assembly into an …

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 …

Abstract The Cullin 5 (CUL5) Ring E3 ligase uses adaptors Elongins B and C (ELOB/C) to
bind different SOCS-box-containing substrate receptors, determining the substrate specificity …

Summary The Cullin-RING E3 ligase (CRL) family is commonly hijacked by pathogens to
redirect the host ubiquitin proteasome machinery to specific targets. During HIV infection …

Background Human immunodeficiency virus type 1 (HIV-1) Vif hijacks an E3 ligase to
suppress natural APOBEC3 restriction factors, and core binding factor β (CBF-β) is required …

Cullin RING E3 ubiquitin ligases (CRLs) function in the ubiquitin proteasome system to
catalyze the transfer of ubiquitin from E2 conjugating enzymes to specific substrate proteins …

ABSTRACT UBR5 is a nuclear E3 ligase that ubiquitinates a vast range of substrates for
proteasomal degradation. This HECT E3 ligase has recently been identified as an important …

Rbx1 and Rbx2 are essential components of Cullin-RING E3 Ligases. Vif is generally
believed to preferentially recruit the Cul5-Rbx2 module to induce proteasomal degradation …

UBR5 is a nuclear E3 ligase that ubiquitinates a vast range of substrates for proteasomal
degradation. This HECT domain‐containing ubiquitin ligase has recently been identified as …

Abstract Cullin RING E3 ligases (CRLs) ubiquitylate hundreds of important cellular
substrates. Here we have assembled and purified the Ankyrin repeat and SOCS Box protein …