 The Sting protein is essential for the type I interferon response triggered by the presence of foreign DNA or self-DNA released from mitochondria or nuclei. When this DNA is detected in the cytoplasm, Sting moves from the endoplasmic reticulum to the Golgi apparatus, where it interacts with the tank-binding kinase 1, TBK1, protein. This interaction leads to the activation of Sting-dependent signaling pathways, resulting in the production of type I interferons. The Sting protein has also been implicated in autoimmune disorders, including Savi syndrome, where mutations in the gene-encoding Sting lead to increased expression of the protein and resultant inflammation. In these cases, TBK1 remains associated with the trans-Golgi network rather than other parts of the Golgi, suggesting that this organelle may serve as a specialized platform for Sting-TBK1 interactions. This article was authored by Haruka Kemoku, Yoshihiko Kuchitsu, Kojiro Mukai, and others.