UBE2E3 Activators

UBE2E3, or ubiquitin-conjugating enzyme E2 E3, operates at the heart of the ubiquitination machinery, a fundamental pathway for protein modification. Influencing the ubiquitination pathway, thereby, offers avenues to modulate UBE2E3's activity. For instance, proteasome inhibitors such as MG132, Bortezomib, Lactacystin, and Velcade underscore the intricate balance between proteasomal degradation and ubiquitination. Their action on proteasomes enhances the ubiquitination process, offering a potential ripple effect on UBE2E3's function.

On a similar note, autophagy inhibitors like Chloroquine, 3-Methyladenine, and Hydroxychloroquine exemplify the interconnected cellular systems. By inhibiting autophagy, these compounds can lead to enhanced ubiquitination, implying a secondary impact on UBE2E3. This balance is further evident with compounds such as PYR-41 and Nutlin-3. While PYR-41, a ubiquitin-activating enzyme E1 inhibitor, directly stimulates ubiquitin-conjugating enzymes, Nutlin-3's activation of the p53 pathway introduces another layer where enhanced p53 can drive ubiquitination.