In addition, this acetylation promoted SHMT2 degradation through the ubiquitin‐lysosome pathway.[14] In another study, sirtuin 5 (SIRT5)‐mediated desuccinylation of SHMT2 increased its activity and drove serine catabolism in cancer cells.[27] SHMT2 was also reported to be a fatty‐acylated protein, and histone deacetylase 11 (HDAC11) mediated its defatty‐acylation.[28] Until now, little has been known about the functions of other posttranslational modifications in regulating SHMT in cancer, especially in lung cancer. This evidence concerns the gene SHMT1 and lung cancer.