SIRT3 Functions as an Eraser of Histone H3K9 Lactylation to Modulate Transcription for Inhibiting the Progression of Esophageal Cancer.

ABSTRACT: Lysine lactylation (Kla) links lactate metabolism to epigenetic regulation, playing a key role in modulation of gene expression in tumor and immune microenvironment. Our recent study shows that HBO1-mediated histone H3K9la activates the transcription of genes encoding tumorigenesis, suggesting the potential significance of intervening in this Kla site for tumor therapy. Evidence so far indicates that traditional deacetylases can catalyze the removal of Kla; however, the precise demodifying enzyme to histone H3K9la in vivo and functional consequence remain elusive. Herein, we combined an antibody-based proximity labeling approach with mass spectrometry analysis to identify SIRT3 as a major binder to histone H3K9la and showed the specific catalysis of SIRT3 for the removal of lactylation. Mo

SUBMITTER: Chen C 

PROVIDER: S-EPMC12144510 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature