PTMScan® Lactyl Lysine Motif (K-La) Kit #83284
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Background
Lactyl lysine exists as two stereoisomers: KL-la and KD-la, though the chief form in mammalian cells is the L stereoisomer KL-la (S configuration). EP300 and KAT2A are among the known enzymes that utilize lactyl-coenzyme A (lactyl-CoA) to lactylate proteins, while SIRT3 and HDAC1 have been documented to remove lactylation (3,4). These enzymes regulate other lysine acyl PTMs, most notably lysine acetylation. However, the regulatory pathways of lactylation differ in several aspects from analogous pathways of acetylation. For example, ACSS2 converts lactate into lactyl-CoA through a cascade of ERK signaling and PIN2 isomerization. While ACSS2 can similarly process acetate into lactyl-CoA, the ACSS2 residues responsible for binding differ from the residues for binding lactate (5). In another example, AARS1 can directly conjugate lactate to proteins without generating a lactyl-CoA donor (6).
Lactate is involved in diverse biological contexts, such as accumulation in brain tissue during cerebral ischemia-reperfusion injury and aerobic glycolysis in cancer. Lactylation roles are likely equally diverse and potentially distinct from acetylation (7). Interestingly, few domains that otherwise bind acetylated lysines have been found to bind lactylated lysines. One known lactyl lysine binder is TRIM33, where a conserved glutamate within the TRIM33 bromodomain is necessary and sufficient for binding to lactylated histones, yet does not affect binding to acetylated histones (8). Differentiating the unique regulation and impact of lactylation from other acyl PTMs remains an active and important area of research.
- Zhang, D. et al. (2019) Nature 574, 575-580.
- Bao, Q. et al. (2024) J Am Soc Mass Spectrom 35, 3221-3232.
- Moreno-Yruela, C. et al. (2022) Sci Adv 8, eabi6696.
- Fan, Z. et al. (2023) iScience 26, 107757.
- Zhu, R. et al. (2025) Cell Metab 37, 361-376.e7.
- Ju, J. et al. (2024) J Clin Invest 134, e174587. doi: 10.1172/JCI174587.
- Shi, P. et al. (2025) Front Cell Dev Biol 13, 1535611.
- Nuñez, R. et al. (2024) ACS Chem Biol 19, 2418-2428.
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