Quantitative proteomic analysis using 4D-FastDIA in gastric cancer cells before and after loss-of-function mutation of STAT1-K193 lactylation.

In this study, we identified a significant lactylation modification at lysine 193 (K193) of STAT1 in gastric cancer tissues through an integrated proteomic and lysine lactylome analysis. Functional assays revealed that the loss of STAT1-K193 lactylation (STAT1-K193la) markedly suppresses gastric cancer cell proliferation, invasion, and metastatic potential. To further elucidate the downstream mechanisms mediated by STAT1-K193 lactylation, we aim to perform comparative proteomic profiling between wild-type STAT1 and the K193 lactylation-deficient mutant. This approach will help identify candidate effector proteins or signaling pathways regulated by STAT1-K193la, which will be subjected to further functional and mechanistic validation to better understand their roles in gastric tumor progression.