STING is established as a central endoplasmic reticulum adaptor in cytosolic DNA sensing. However, its functional capacity beyond immune activation is yet to be explored. While recent studies have revealed its critical role in non-canonical autophagy independent of its immunity functions, its role in selective autophagy remains elusive. Here, we revealed that STING translocate to depolarized mitochondria in a PINK1-Parkin-dependent manner. Strikingly, STING operates as a molecular linchpin coordinating two critical events: (1) recruitment of the selective autophagy receptor OPTN to damaged mitochondria, and (2) enabling TBK1-mediated OPTN phosphorylation and the ultimate clearance of damaged mitochondria in lysosome. Disruption of the STING-OPTN axis impairs mitophagy, which switches cellular response from mitophagy to apoptosis. Our findings thus reveal a novel function of STING that couples mitochondrial health surveillance with mitophagy, which is essential for cell fate decisions.