Histone and non-histone lactylation: molecular mechanisms, biological functions, diseases, and therapeutic targets

Lysine lactylation (Kla) is a recently discovered post‑translational modification in which a lactyl moiety is transferred onto the ε‑amino group of lysine residues, linking cellular metabolism to epigenetic and signaling pathways. This process is regulated by a range of enzymes and metabolites, including lactate, "lactyltransferases (writers)", "Delactylases (erasers)", and "readers" involved in the modification. Histone lactylation has been observed in H2A, H2B, H3, and H4, with H3K18la and H4K12la being the most extensively studied sites, linked to numerous biological functions. Beyond chromatin, Kla has also been identified in a growing number of non-histone proteins, further expanding its functional…

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  National Natural Science Foundation of China

  Awards: 82370910, 82170912