Inspired by recent studies that reported ubiquitin-mediated proteolysis of key signaling proteins 33-36 and our finding of physical interaction between SDC2 and ubiquitin-specific protease 14 (USP14), we evaluated the effect of USP14 in regulating the abundance of SDC2 in GC, and assessed the possible therapeutic utility of IU1, a small-molecule inhibitor that increases the ubiquitination-mediated degradation of SDC2 by targeting USP14. This evidence concerns the gene SDC2 and gastric cancer.