STING (stimulator of interferon genes) is a novel regulatory protein in innate immune signaling pathways, which has been shown to be essential for the production of type Ⅰ interferon in response to certain viruses and intracellular bacteria. B type dsDNA and 5′-3p dsRNA are detected by the corresponding pattern recognition receptors (PRRs) after exposing to host cells, which pass signals to STING. STING then recruits TBK1 to activate IRF3 and induce IFN by the similar mechanism. Besides, STING can be a PRR of the cyclic dinucleotides, such as c-di-GMP and c-di-AMP in bacteria, to induce type Ⅰ interferon response. Except IFN, STING also activates STAT6 to induce some specific chemokines capable of attracting various immune cells. Here, we review recent studies on STING's structure, location, function, and regulatory mechanisms in the innate immune pathway, which provide an important theoretical guidance for the development of new antiviral immunotherapy.