This entry includes protein zyg-11 homologue B from vertebrates. In Caenorhabditis elegans, Zyg-11 (not included in this entry) is the substrate-recognition subunit for a CUL-2-based complex that regulates several key processes in cell division and embryonic development []. Similarly, the CRL2-ZYG11 complex in humans acts as a ubiquitin ligase and is comprised of the cullin CUL2, the RING finger protein Rbx1/Roc1, the adaptor subunit Elongin C, and ZYG-11 orthologues ZYG11A or ZYG11B. In human cells, the CRL2ZYG11A/B-mediated degradation of cyclin B1 facilitates mitotic slippage in cells in which APC/C is inactive []. The ZYG11B-based E3 ubiquitin ligase complex mediates polyubiquitination of the cell cycle-regulated protein ZFP36L2 []. ZYG11B targets substrates bearing N-terminal glycine degrons for proteasomal degradation and it is also involved in the quality control of protein N-myristoylation in which N-terminal glycine degrons are exposed after a failure of N-myristoylation [].
