Sentrin-specific protease 7 (SENP7)

Sentrin-specific protease 7 (SENP7) is an enzyme in the SUMO-specific protease family, specialized in catalyzing the removal of poly-SUMO2/3 chains from substrate proteins, thereby regulating protein stability, localization, and function[2][3][4]. SENP7 plays critical roles in immune cell metabolism—particularly in CD8+ T cells—by sensing oxidative stress and promoting metabolic and antitumor functions through deSUMOylation of PTEN[1]. It also acts as a positive regulator of the innate immune cGAS-STING pathway by desumoylating the DNA sensor cGAS, facilitating its DNA-binding activity[4]. In cancer, SENP7 has been shown to inhibit invasion and angiogenesis in glioblastoma and is linked to immune cell fitness in colorectal cancer[1][3]. SENP7 is considered a potential therapeutic target for precision cancer therapies, although no specific direct inhibitors are currently in clinical use[3].

Other names

KIAA1707SSP2SUSP2SUMO-1-specific protease 2SUMO1/sentrin-specific peptidase 7sentrin/SUMO-specific protease SENP7

Catalyzes removal of SUMO2/3 chains from substrate proteins, regulating downstream signaling, protein interactions, and degradation[2][3][4]. In T cells, prevents PTEN-dependent metabolic defects by promoting PTEN degradation[1]. Regulates cGAS DNA-binding activity by desumoylating cGAS, promoting cGAS-STING-mediated signaling[4].