UBE3C アクチベーター

The functional mechanisms of UBE3C activators center around their indirect effects on cellular pathways, leading to enhanced ubiquitination activity of UBE3C. These compounds influence various cellular processes, such as proteasomal inhibition, ER stress, and cellular stress responses, which in turn can indirectly stimulate UBE3C's functional activity. Compounds like Geldanamycin and Bortezomib act by inhibiting the function of Hsp90 and the proteasome, respectively. This leads to an increased accumulation of proteins requiring ubiquitination, indirectly necessitating heightened activity of ubiquitin-protein ligases like UBE3C.

Similarly, Tunicamycin and Thapsigargin induce ER stress by inhibiting N-linked glycosylation and disrupting calcium homeostasis. The resulting activation of the unfolded protein response creates a demand for enhanced activity of proteins involved in degrading misfolded proteins, including UBE3C. On the other hand, Lactacystin and Beta-Lactone, which target the proteasome, lead to the accumulation of ubiquitinated proteins. This accumulation acts as a signal for the cell to enhance its ubiquitination processes, indirectly stimulating UBE3C's role in tagging proteins for degradation.