ZNF213 Inhibitors

Compounds such as MG132, Bortezomib, Epoxomicin, and Lactacystin interfere with the ubiquitin-proteasome system, an essential pathway for protein degradation. By modulating the degradation processes, these inhibitors can lead to the accumulation of proteins that directly or indirectly interact with ZNF598, potentially altering its role in ribosome-associated quality control and nonsense-mediated mRNA decay.

Translation inhibitors like Cycloheximide, Puromycin, and Emetine directly engage with the translation machinery, a key area of ZNF598's activity. These compounds can prevent the proper functioning of the ribosome, which is closely monitored by ZNF598. In doing so, they may inadvertently impact ZNF598's ability to regulate the quality of protein synthesis. Similarly, mTOR signaling is crucial for ribosomal biogenesis and protein synthesis, and its inhibition by Rapamycin can lead to changes in the cellular environment that influence ZNF598's activity. Furthermore, Actinomycin D and α-Amanitin exert their effects by disrupting RNA synthesis, which can lead to changes in the levels of RNA substrates available for ZNF598 to act upon. Chloroquine's impact on autophagy and lysosomal degradation also can modulate protein turnover, affecting ZNF598 activity indirectly. Leptomycin B's inhibition of RNA export can influence the nuclear roles of ZNF598, potentially impacting its regulatory functions.