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EMBO Rep. 2018 Oct;19(10). pii: e46666. doi: 10.15252/embr.201846666. Epub 2018 Sep 19.

Protein palmitoylation and cancer.

Author information

1
Department of Biology, Stanford University, Stanford, CA, USA.
2
Department of Biology, Stanford University, Stanford, CA, USA sjdixon@stanford.edu.

Abstract

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.

KEYWORDS:

S‐palmitoylation; lipid; lipidation; post‐translational modification; tumor

PMID:
30232163
PMCID:
PMC6172454
[Available on 2019-10-01]
DOI:
10.15252/embr.201846666

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