RING proteins constitute the largest class of E3 ubiquitin ligases. Unlike most RINGs, AO7
(RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high …

RING finger proteins constitute the large majority of ubiquitin ligases (E3s) and function by
interacting with ubiquitin‐conjugating enzymes (E2s) charged with ubiquitin. How low …

E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating
transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate. The activity of …

RING E3 ligase–catalyzed formation of K63-linked ubiquitin chains by the Ube2V2–Ubc13
E2 complex is required in many important biological processes. Here we report the structure …

Ubiquitin-mediated proteolysis utilizes a series of three key enzymes (E1, E2, and E3) to
transfer and then covalently modify a substrate with ubiquitin. E2 conjugating enzymes are …

The interplay between E2 and E3 enzymes regulates the polyubiquitination of substrates in
eukaryotes. Among the several RING-domain E3 ligases in humans, many utilize two distinct …

The activity of RING ubiquitin ligases (E3s) depends on an interaction between the RING
domain and ubiquitin conjugating enzymes (E2), but posttranslational events or additional …

Abstract RING-between-RING (RBR) ubiquitin ligases work with multiple E2 enzymes and
function through an E3-ubiquitin thioester intermediate. The RBR module comprises three …

Abstract The RING-between-RING (RBR) E3 ubiquitin ligase family in humans comprises 14
members and is defined by a two-step catalytic mechanism in which ubiquitin is first …

Substantial evidence has accumulated indicating a significant role for oligomerization in the
function of E3 ubiquitin ligases. Among the many characterized E3 ligases, the yeast U-box …