SUMO-specific peptidase 3 (SENP3)

SUMO-specific peptidase 3 (SENP3) is an enzyme that catalyzes the removal (deSUMOylation) of SUMO2/3 groups from various proteins, modulating their activity, localization, and stability[1][4]. SENP3 acts as a redox sensor, integrating oxidative stress signals to regulate the SUMOylation status of critical cellular proteins, impacting processes such as transcription (via targets like p300 and HIF-1α), mitochondrial fission (through Drp1 and FIS1), mitophagy, and ribosome biogenesis (via NPM1/B23) [1][3][4]. SENP3 plays a central role in maintaining genome integrity, cell cycle progression, and adaptive responses to cellular stress. Dysregulation or overexpression of SENP3 is associated with various cancers and metabolic or inflammatory diseases[1][4]. SENP3 is recognized as a potential therapeutic target due to its pivotal regulatory roles, but targeting it presents challenges stemming from its involvement in essential and diverse cellular pathways[1][4][3]. If you require information on known direct pharmacological inhibitors or drugs in clinical development specifically modulating SENP3, there are currently no established drugs or clinical candidates reported in the search results.

Other names

Sentrin-specific protease 3SSP3SUSP3DKFZP586K0919DKFZp762A152SMT3IP1Ulp1SUMO-1-specific protease 3sentrin/SUMO-specific protease SENP3SUMO1/sentrin/SMT3 specific peptidase 3Five Friends of Methylated CHTOP (5FMC) component

Inhibition or modulation of deSUMOylation activity; Regulation of SUMO conjugation states on target proteins (e.g., influencing transcription factors, mitochondrial proteins)