Lactylation shields S100A11 from degradation to promote gastric cancer metastasis.

ABSTRACT:

Background

Protein lactylation, a novel post-translational modification utilizing lactate as the substrate, has emerged as a key mechanism linking metabolic alterations to cancer progression. This study aims to investigate the role and underlying mechanism of S100A11 lactylation in gastric cancer progression and metastasis.

Methods

Lactylome profiling, site-directed mutagenesis, co-IP, cycloheximide chase, ubiquitination assays, and in vitro/in vivo functional experiments were performed to dissect the regulatory effect of S100A11 lactylation.

Results

S100A11 was identified as a hyperlactylated protein in gastric cancer tissues, with lysine 27 (K27) and lysine 55 (K55) serving as the primary modification sites. Mechanistically, lactylation at K27 and K55 disrupted the

SUBMITTER: Zhang Q 

PROVIDER: S-EPMC13631184 | biostudies-literature | 2026 Jul

REPOSITORIES: biostudies-literature