UBCH10 Inhibitors

UBCH10 inhibitors are a class of compounds that specifically target and modulate the activity of the enzyme UBCH10, also known as UBE2C, a member of the ubiquitin-conjugating enzyme family. UBCH10 plays a crucial role in the ubiquitin-proteasome system (UPS), which is responsible for regulating protein degradation within cells. In particular, UBCH10 is involved in the anaphase-promoting complex/cyclosome (APC/C)-mediated ubiquitination of specific proteins that control cell cycle progression, especially during the metaphase-anaphase transition in mitosis. The inhibition of UBCH10 activity can significantly affect the ubiquitination process, thereby altering the timing and regulation of cellular events such as chromosome segregation and mitotic exit.

By modulating the activity of UBCH10, inhibitors of this enzyme can lead to disruptions in the tightly regulated processes of protein turnover and cell cycle control. These inhibitors tend to act by binding to the active site or nearby regions of UBCH10, preventing the transfer of ubiquitin to target substrates. This results in the accumulation of specific proteins that would normally be degraded, affecting the downstream processes that are dependent on protein degradation for their regulation. Given the critical nature of UBCH10 in cell cycle control and protein homeostasis, these inhibitors offer a valuable tool for studying ubiquitination dynamics and the mechanistic roles of UBCH10 in proteostasis and mitotic regulation. Additionally, the structural diversity of UBCH10 inhibitors enables the exploration of various binding modalities and selectivity profiles in the context of ubiquitin-conjugating enzyme function.