EG628518 Inhibitors

The class of chemicals identified as Ctag2l2 inhibitors encompasses a range of compounds that can influence the activity of the protein Ctag2l2 by various mechanisms. Tunicamycin, for example, can disrupt glycosylation processes within the cell, which is essential for the proper folding and stability of proteins like Ctag2l2, particularly within the context of the EKC/KEOPS complex. Similarly, cycloheximide and emetine are known to inhibit protein synthesis by interfering with the translocation and elongation steps on ribosomes, respectively, thereby reducing the synthesis of proteins such as Ctag2l2. This can lead to a decrease in the protein's availability within the cellular milieu. Additionally, chloroquine can alter the pH and environment of organelles such as the centrosome, affecting the activity or interactions of Ctag2l2 localized in that region.

On the other hand, deoxyglucose can lead to a depletion of cellular energy levels, which can impact energy-dependent processes involving Ctag2l2. Actinomycin D binds to DNA, preventing the transcription of proteins part of the EKC/KEOPS complex, including Ctag2l2. Puromycin causes premature chain termination during protein synthesis, leading to a reduction in the full-length Ctag2l2 protein. Rapamycin can inhibit mTOR signaling, which regulates protein synthesis and, by extension, can affect the assembly or function of the EKC/KEOPS complex. Furthermore, 5-Fluorouracil can interfere with the synthesis and modification of tRNAs, processes in which Ctag2l2 is implicated. Hydroxyurea can affect DNA synthesis and repair, which in turn can alter the synthesis of the EKC/KEOPS complex proteins. Nocodazole can disrupt microtubule polymerization, which can affect the function of Ctag2l2 within the centrosome. Finally, compounds like trimethoprim, although used to target bacterial enzymes, suggest that analogs targeting human enzymes can be designed to affect similar pathways involving the EKC/KEOPS complex and Ctag2l2.