| First Author | Ko PJ | Year | 2018 |
| Journal | EMBO Rep | Volume | 19 |
| Issue | 10 | PubMed ID | 30232163 |
| Mgi Jnum | J:266761 | Mgi Id | MGI:6201975 |
| Doi | 10.15252/embr.201846666 | Citation | Ko PJ, et al. (2018) Protein palmitoylation and cancer. EMBO Rep 19(10) |
| abstractText | Protein S-palmitoylation is a reversible post-translational modification that alters the localization, stability, and function of hundreds of proteins in the cell. S-palmitoylation is essential for the function of both oncogenes (e.g., NRAS and EGFR) and tumor suppressors (e.g., SCRIB, melanocortin 1 receptor). In mammalian cells, the thioesterification of palmitate to internal cysteine residues is catalyzed by 23 Asp-His-His-Cys (DHHC)-family palmitoyl S-acyltransferases while the removal of palmitate is catalyzed by serine hydrolases, including acyl-protein thioesterases (APTs). These enzymes modulate the function of important oncogenes and tumor suppressors and often display altered expression patterns in cancer. Targeting S-palmitoylation or the enzymes responsible for palmitoylation dynamics may therefore represent a candidate therapeutic strategy for certain cancers. |
