CUL3

(redirected from cullin-3)

CUL3

A gene on chromosome 2q36.2 that encodes cullin-3, a core protein of multiple cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Cullin-3 may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The ubiquitin-protein ligase activity of the complex depends on neddylation of the cullin subunit, and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1.
References in periodicals archive ?
To ascertain how Cullin-3 based ubiquitination and proteasome degradation facilitate the switch from uncoating to replication of the viral genome, we will identify the relevant Cullin-3 substrates in the context of a detailed characterization of viral replication initiation sites.
OBJECTIVE: We investigated the cross-regulations among NRF2, NRF1, and KEAP1, a cullin-3 adapter protein that allows NRF2 to be ubiquinated and degraded by the proteasome complex, in arsenic-induced antioxidant responses.
Kelch-like ECH-associated protein 1 (KEAP1), a cytoplasmic protein, serves as a substrate-adaptor molecule for cullin-3 based ubiquitin E3 ligase (Kobayashi et al.
Under normal physiological conditions, Keap1, which is also called an inhibitor of Nrf2 (INrf2), is associated with Nrf2 (the majority of which resides in the cytoplasm) and recruits and interacts with the cullin-3 E3-ubiquitin ligase (Cul3) [77].
Additionally, numerous reports have suggested that Kelch-like ECH-associated protein-1 (Keap1), a substrate adaptor protein for a cullin-3 E3-ubiquitin ligase (Cul3)/Ring-Box1 (Rbx1) dependent complex, plays a critical role in the ubiquitination and degradation of Nrf2, IKK[beta], and Bcl-2/Bcl-xL, also being disturbed by ROS via modifying the reactive cysteines (Cys273, Cys288, and Cys151) and then inducing a conformational change that leads to the release of Nrf2, IKK[beta], and Bcl-2/Bcl-xL from Keap1 and the suspending of their ubiquitination and degradation [172-174].