Abstract
Ubiquitylation helps regulate protein degradation and maintain normal cellular function. E3 ubiquitin ligases facilitate the attachment of ubiquitin molecules to substrate proteins. The most common class of E3 ubiquitin ligase is the Cullin RING Ligase (CRL), which is a complex of proteins containing a Cullin protein as a scaffold. Cullin 5 associates with one of 18 Ankyrin-Repeat and SOCS Box (ASB) proteins, and the RING-box (RXB) protein, RBX2 which binds the ubiquitylated E2. When substrate binds, the ubiquitin is transferred from the E2 protein to an exposed lysine residue on the substrate.
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