USP31 Activators

USP31 Activators are a class of compounds that interact with cellular pathways, leading to the enhancement of the deubiquitinating enzyme USP31's functional activity. These compounds, while not directly interacting with USP31, play a role in modulating the ubiquitination status of proteins within the cell, thus creating a demand for USP31 activity. Proteasome inhibitors like Epoxomicin and MG132 lead to the accumulation of ubiquitinated proteins, which can indirectly enhance the functional activity of USP31 by increasing the substrate availability for deubiquitination. Similarly, the inhibition of other ubiquitin-specific proteases, such as with P22077 or HBX 41,108, might result in a compensatory upregulation of USP31's activity to maintain cellular protein homeostasis.

On the other hand, compounds like PYR-41 and IU1 target upstream components of the ubiquitination cascade, such as the ubiquitin-activating enzyme E1 and USP14, respectively. The inhibition of these enzymes can lead to a reduced ubiquitination rate, which, in turn, may necessitate an increase in USP31 activity to rebalance the ubiquitination-deubiquitination dynamics. Inhibitors like b-AP15 and VLX1570 disrupt the function of proteasome-associated DUBs, thereby enhancing USP31 activity as a parallel response to ensure the continuous regulation of protein degradation.