EGFR and cancer: Although the palmitoylated status of PD-L1 has been exclusively attributed to the catalytic activity of tissue cancer-specific palmitoyl acyltransferases containing Asp-His-His-Cys (DHHC) in the active center, it should be acknowledged that FASN activity may contribute to the de novo synthesis and intracellular accumulation of palmitoyl-CoA in the range of 0.1–10 μmol/L to serve as a palmitoylation donor of several cancer-related proteins (e.g., EGFR, MYD88, AKT, tubulin) [75–77, 114–117].