Research has found that LKB1 can be phosphorylated, deacetylated, and ubiquitinated under different conditions.[39, 40, 41] Several kinases, such as protein kinase A (PKA), protein kinase C (PKC), and ataxia‐telangiectasia mutated (ATM), have been reported to phosphorylate LKB1.[39, 42] SIRT2 has been shown to bind and deacetylate LKB1 to attenuate angiotensin II‐induced cardiac hypertrophy.[40] LKB1 can be post‐translationally modified by ubiquitination and deubiquitination, but not by phosphorylation or prenylation. The gene discussed is SIRT2; the disease is cardiac hypertrophy.