KLHL24 Activators

KLHL24 Activators are a class of compounds that, through their influence on the ubiquitin-proteasome system and cellular autophagy processes, can indirectly enhance the functional activity of KLHL24. Since KLHL24 is implicated in the specific tagging of substrates for ubiquitination, compounds like MG132 and Lactacystin, which inhibit the proteasome, can lead to the buildup of ubiquitinated proteins. This accumulation may signal a cellular need for increased ubiquitin ligase activity, thereby enhancing KLHL24 function. Similarly, IU1, which targets USP14, an enzyme responsible for trimming ubiquitin chains from proteins, can maintain or increase the pool of ubiquitinated proteins, indirectly necessitating the function of ubiquitin ligases such as KLHL24.

Furthermore, compounds like Pyr-41, SMER3, and Chloroquine modulate different aspects of the ubiquitination and autophagy pathways, which are interconnected with protein degradation processes. Pyr-41's inhibition of the ubiquitin-activating enzyme E1 can lead to an increased need for ubiquitin-protein conjugation, a step in which KLHL24 could play a role. SMER3, by enhancing autophagy, may influence the degradation pathways and upregulate the ubiquitination system as a compensatory mechanism, thereby involving KLHL24. Chloroquine, an autophagy inhibitor, may cause cells to rely more heavily on the ubiquitin-proteasome system, indirectly increasing KLHL24's role.