Furthermore, we delineate how lactylation signals are interpreted by specific readers (e.g., TRIM33), directly reprogram non-histone protein function through structural metamorphosis (e.g., disrupting p53, enhancing XLF), and engage in complex crosstalk with other PTMs, as exemplified by the synergistic interplay between histone H3 lysine 18 lactylation (H3K18la) and histone H3 lysine 27 acetylation (H3K27ac) in T-cell acute lymphoblastic leukemia (T-ALL). This evidence concerns the gene TP53 and acute lymphoblastic leukemia.