The Stimulator of Interferon Genes (STING) protein is an integral component of the innate immune system, known for its role in mediating immune signaling pathways. Under normal conditions, STING resides in the endoplasmic reticulum (ER), and its activation is initiated through the cGAS-STING signaling pathway. Upon activation, STING is trafficked to the Golgi apparatus, which sets off a series of downstream signaling events. STING's journey from the ER to the Golgi apparatus is vital for its activation of downstream signaling pathways. Post-translational modifications, such as palmitoylation and phosphorylation, play a significant role in the trafficking and function of STING. The STING protein is also subject to regulation through ubiquitination, which is involved in its trafficking between the ER and Golgi apparatus. The E3 ubiquitin ligase RNF144 facilitates the K6-linked ubiquitination of STING, enhancing its transport. Furthermore, research has indicated that STING is involved in various cellular processes beyond the immune response, including autophagy, ER stress response, and metabolic reprogramming. After activation, STING is transported into small extracellular vesicles, where it can be recognized by the STAM protein, leading to the termination of STING signaling.