Global Profiling of Protein Lactylation, Crotonylation, Succinylation and Phosphorylation in Lung Adenocarcinoma Cell.

The novel protein acylation modifications have played a vital role in protein post-translational modifications. However, the functions and effects of the protein acylation modifications in lung adenocarcinoma are still uncertain. Currently, there is also a lack of global identification of acylation modifications in lung adenocarcinoma cells. Therefore, in this study, we detected 10 currently known acylation modifications in lung adenocarcinoma cells by western blot. Interestingly, we found that the abundance of lysine succinylation (Ksu), crotonylation (Kcr) and lactylation (Kla) is likely higher. Immediately, we identified the above three modifications and phosphorylation by global mass spectrometry-based proteomics in lung adenocarcinoma cells. As a result, we got 3110 Kla sites in 1220 lactylated proteins, 16653 Kcr sites in 4137 crotonylated proteins, 4475 Ksu sites in 1221 succinylated proteins, and 15254 phosphorylation sites in 4139 phosphorylated proteins. In conclusion, our results provide a proteome-wide database to study Kla, Kcr and Ksu and phosphorylation in lung adenocarcinoma, and our bioinformatics results provide new insights into the role of acylation modification in lung adenocarcinoma.