Using APEX2-mediated proximity labeling of SARS-CoV-2 nsp3, we identified the GBF1 as a key interacting protein within DMVs. Functional disruption of GBF1 or COPI not only suppressed viral RNA synthesis but also significantly reduced the size and abundance of DMVs and inhibits Golgi-DMVs colocalization. Imaging and biochemical assays further confirmed coronavirus infection induced redistribution of Golgi membranes to DMV formation sites. Our study demonstrates that coronaviruses exploit the GBF1-ARF1-COPI pathway to hijack COPI vesicles for the generation of DMVs, providing a mechanistic foundation for targeting this host secretory pathway as a therapeutic strategy against coronavirus infections.