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

ABSTRACT: 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.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Duanrui Liu

LAB HEAD: Duanrui Liu

PROVIDER: PXD065104 | Pride | 2025-09-05

REPOSITORIES: Pride

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			Action	DRS
	Result.zip	Other
	XA08562DA_K193_1_Slot1-27_1_30490.d.zip	Other
	XA08562DA_K193_2_Slot1-28_1_30491.d.zip	Other
	XA08562DA_K193_3_Slot1-29_1_30492.d.zip	Other
	XA08562DA_WT_1_Slot1-24_1_30486.d.zip	Other

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