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. Here, SIRT5 is linked to lung carcinoma.