Class I histone deacetylases catalyze lysine lactylation.

ABSTRACT: Metabolism and post-translational modifications (PTMs) are intrinsically linked, and the number of identified metabolites that can covalently modify proteins continues to increase. This metabolism/PTM crosstalk is especially true for lactate, the product of anaerobic metabolism following glycolysis. Lactate forms an amide bond with the ε-amino group of lysine, a modification known as lysine lactylation or Kla. Multiple independent mechanisms have been proposed in the formation of Kla, including p300/CBP-dependent transfer from lactyl-CoA, a reactive intermediate lactoylglutathione species that non-enzymatically lactylates proteins, and several enzymes are reported to have lactyl transferase capability. We recently discovered that class I histone deacetylases (HDACs) 1, 2, and 3 can all rev

SUBMITTER: Gonzatti MB 

PROVIDER: S-EPMC12624779 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature