SENP2 Activators

SENP2 activators represent a diverse group of chemicals that modulate the activity of SENP2 through various pathways and cellular processes. MLN4924, a NEDD8-activating enzyme (NAE) inhibitor, indirectly activates SENP2 by preventing the neddylation of proteins. This inhibition alters post-translational modifications, including changes in SUMOylation, creating conditions favorable for SENP2 activation. Nutlin-3, a p53 stabilizer, indirectly activates SENP2 by stabilizing p53 and promoting its interaction with SENP2, modulating the p53 pathway and influencing SENP2-dependent deSUMOylation events. C646, a histone acetyltransferase p300/CBP inhibitor, indirectly activates SENP2 by inhibiting p300/CBP-mediated acetylation events, creating conditions conducive to SENP2-dependent deacetylation. Pargyline, an MAO-B inhibitor, indirectly activates SENP2 by inhibiting MAO-B activity, modulating the sumoylation status of proteins associated with the MAO-B pathway. JIB-04, a histone demethylase inhibitor, indirectly activates SENP2 by inhibiting histone demethylases, creating conditions conducive to SENP2-dependent deSUMOylation events.

RSL3, a ferroptosis inducer, indirectly activates SENP2 by inhibiting GPX4, influencing the desumoylation and stabilization of proteins involved in ferroptosis. Niclosamide, influencing Wnt/β-catenin signaling, leads to alterations in the sumoylation status of proteins associated with Wnt/β-catenin signaling, activating SENP2. BAY 11-7082, an NF-κB inhibitor, indirectly activates SENP2 by inhibiting NF-κB activation, modulating the sumoylation status of proteins associated with the NF-κB pathway. Sirtinol, a sirtuin inhibitor, indirectly activates SENP2 by inhibiting SIRT1, modulating the sumoylation status of proteins regulated by SIRT1. Cyclopamine, a Hedgehog signaling pathway inhibitor, indirectly activates SENP2 by inhibiting Hedgehog signaling, modulating the sumoylation status of proteins associated with this pathway. These SENP2 activators showcase the intricate network of cellular processes and signaling pathways through which SENP2 function can be modulated, providing insights into the complex regulation of post-translational modifications and protein stability in diverse cellular contexts.