In mammalian cells, the S-palmitoylation to internal cysteine residues is modulated by a family of 23 zinc finger Asp-His-His-Cys (DHHC) domain-containing (ZDHHC) protein acyltransferase (PATs) (Fukata et al., 2006). To identify novel S-palmitoylation substrates in LUAD, systemically evaluation of the ZDHHC family for the key ZDHHC is necessary. Previously, most ZDHHC proteins were found to localize to the plasma membrane, endoplasmic reticulum, and the Golgi apparatus (Ko and Dixon, 2018). However, recently, nucleoproteins of transcription factors (Chan et al., 2016), chromatin remodelers (Riccio, 2010), and histone proteins (Wilson et al., 2011) have been proposed as targets for palmitoylation (Spinelli et al., 2018). Therefore, nucleus-targeting S-palmitoylation may provide insight into novel strategies for cancer therapy.
