E3 Ubiquitin Ligase (None)

E3 ubiquitin ligases are a large and diverse family of enzymes that play a central role in the ubiquitination process, which is a post-translational modification critical for regulating protein stability, function, and localization in eukaryotic cells. They act as the final component in a three-enzyme cascade—alongside E1 (ubiquitin-activating enzyme) and E2 (ubiquitin-conjugating enzyme)—to catalyze the transfer of ubiquitin from an E2 enzyme to specific lysine residues on substrate proteins. Ubiquitination regulates numerous cellular processes including protein degradation via the 26S proteasome, cell cycle progression, DNA repair, endocytosis, transcriptional regulation, and response to cellular stress. Dysregulation or mutation of E3 ligases is implicated in various diseases such as cancer. Inhibitors or modulators targeting specific disease-associated or dysregulated E3s are under investigation for drug development.

Inhibition or modulation of E3 ligase activity, or PROTAC-mediated degradation of target proteins