Stimulator of interferon genes protein (STING) (STING)

The Stimulator of Interferon Genes (STING) is a central transmembrane adaptor protein located in the endoplasmic reticulum that plays a critical role in the innate immune system by sensing cytosolic nucleic acids. It is primarily activated by cyclic GMP-AMP (cGAMP), which is produced by the enzyme cGAS upon detection of double-stranded DNA in the cytosol, a signal typically associated with viral infection or cellular damage. Once activated, STING undergoes a conformational change and translocates to the Golgi apparatus, where it recruits TANK-binding kinase 1 (TBK1) to phosphorylate interferon regulatory factor 3 (IRF3), leading to the robust induction of Type I interferons and other pro-inflammatory cytokines. In oncology, STING agonists are being developed to 'turn cold tumors hot' by promoting dendritic cell activation and T-cell recruitment within the tumor microenvironment. Conversely, overactivation of the STING pathway is linked to various autoinflammatory diseases, making STING inhibitors a focus for treating conditions like lupus and SAVI. Note: The provided target name 'STING pathway and intracellular nucleic acid sensors' refers to a complex signaling network rather than a single molecular entity, though STING is its primary therapeutic focal point.

Other names

TMEM173ERISMITAMPYSNET23Stimulator of interferon genes pathwaycGAS-STING pathway

STING agonists bind to the STING dimer, inducing a conformational change that leads to the recruitment and activation of TBK1 and IRF3, ultimately triggering the production of Type I interferons and pro-inflammatory cytokines to enhance anti-tumor immunity. Conversely, STING antagonists inhibit this activation to treat inflammatory and autoimmune conditions.