The chemical class known as CUEDC2 Activators encompasses a group of compounds that have the potential to indirectly influence the activity or function of CUEDC2 (CUE domain-containing 2), a protein involved in various cellular processes, including the regulation of ubiquitination and protein degradation.
One strategy employed by CUEDC2 activators is the inhibition of proteasomal degradation, a process critical for the turnover of ubiquitinated proteins. Compounds such as MG-132 and Lactacystin, both proteasome inhibitors, play a pivotal role in this regard. By preventing the degradation of proteins tagged for ubiquitination, these compounds indirectly stabilize the interactions between CUEDC2 and ubiquitinated proteins, potentially enhancing CUEDC2-mediated regulatory functions within the ubiquitin-proteasome system. Additionally, CUEDC2 activators include chemicals like AICAR and Rapamycin, which act on upstream signaling pathways. AICAR activates AMP-activated protein kinase (AMPK), influencing cellular energy levels and the ubiquitination of specific protein substrates. Rapamycin, on the other hand, inhibits the mTOR pathway, a central regulator of protein synthesis and degradation. Through the suppression of mTOR, Rapamycin indirectly impacts CUEDC2-mediated processes related to protein turnover.
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