Dynamic investigation of hypoxia-induced L-lactylation.

ABSTRACT: The recently identified histone modification lysine lactylation can be stimulated by L-lactate and glycolysis. Although the chemical group added upon lysine lactylation was originally proposed to be the L-enantiomer of lactate (K_L-la), two isomeric modifications, lysine D-lactylation (K_D-la) and N-ε-(carboxyethyl) lysine (K_ce), also exist in cells, with their precursors being metabolites of glycolysis. The dynamic regulation and differences among these three modifications in response to hypoxia remain poorly understood. In this study, we demonstrate that intracellular K_L-la, but not K_D-la or K_ce, is up-regulated in response to hypoxia. Depletion of glyoxalase enzymes, GLO1 and GLO2, had minimal impact on K_D-la, K<

SUBMITTER: Gao J 

PROVIDER: S-EPMC11912421 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature