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　ITN　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.