Core component of multiple cullin-RING-based E3 ubiquitin- protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:
14578910, PubMed:
16322693, PubMed:
16678110, PubMed:
18593899, PubMed:
29779948, PubMed:
30166453, PubMed:
33854232, PubMed:
33854239, PubMed:
22118460). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (PubMed:
14578910, PubMed:
16678110, PubMed:
18593899, PubMed:
29779948, PubMed:
22118460). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin- conjugating enzyme (PubMed:
14578910, PubMed:
16678110, PubMed:
18593899, PubMed:
22118460). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage (PubMed:
14578910, PubMed:
16678110, PubMed:
18593899). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication (PubMed:
16678110). A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:
29779948). The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:
33854232, PubMed:
33854239). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:
30166453). Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (PubMed:
16322693, PubMed:
19801544). Regulates the mammalian target-of- rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism (PubMed:
18235224). Specific CUL4B regulation of the mTORC1- mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (PubMed:
18235224). With CUL4A, contributes to ribosome biogenesis (PubMed:
26711351).
