USP3 Activators

USP3 Activators are a collection of chemical compounds that enhance the functional activity of USP3 through indirect means, influencing various cellular pathways that USP3 is associated with. Betulinic acid serves as a pivotal activator by inhibiting USP3's deubiquitinating activity on p53, leading to an indirect enhancement of p53's ubiquitination and activation, which is part of the cellular stress response. Proteasome inhibitors like MG132 also play a unique role by increasing the ubiquitinated proteins within the cell, thereby potentially elevating the functional demand for USP3's deubiquitinating activity. Similarly, PYR-41's inhibition of the E1 ubiquitin-activating enzyme leads to a build-up of ubiquitinated proteins that may also indirectly increase the activity of USP3. IU1, by inhibiting USP14, andUSP3 Activators are a collection of chemical compounds that enhance the functional activity of USP3 through indirect means, influencing various cellular pathways that USP3 is associated with. Betulinic acid serves as a pivotal activator by inhibiting USP3's deubiquitinating activity on p53, leading to an indirect enhancement of p53's ubiquitination and activation, which is part of the cellular stress response. Proteasome inhibitors like MG132 also play a unique role by increasing the ubiquitinated proteins within the cell, thereby potentially elevating the functional demand for USP3's deubiquitinating activity. Similarly, PYR-41's inhibition of the E1 ubiquitin-activating enzyme leads to a build-up of ubiquitinated proteins that may also indirectly increase the activity of USP3. IU1, by inhibiting USP14, and G5, by inhibiting USP7, alter the deubiquitinating enzyme landscape, possibly leading to a compensatory increase in USP3 activity to maintain protein homeostasis.

Further enhancing the spectrum of USP3 activators, compounds like NSC697923, LDN-57444, and b-AP15 selectively target other deubiquitinases such as USP24, UCHL5, and the 19S regulatory particle's deubiquitinating components, respectively. This selective inhibition may redirect substrate proteins towards USP3, thus potentially boosting its activity. WP1130, with its unique action on several USPs including USP9x and USP5, may similarly enhance USP3's role by reducing its competition for substrates. Additionally, HBX 41,108 and P22077, which target USP7 and USP47, alongside SJB2-043, an inhibitor of USP1, may contribute to the enhancement of USP3's deubiquitinating activities by increasing the ubiquitinated protein load. Collectively, these activators, through their targeted effects on cellular deubiquitination processes, serve to indirectly but effectively augment the functional activity of USP3, a crucial player in protein regulation and cellular homeostasis.