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Protein palmitoylation and cancer
Author(s) -
Ko PinJoe,
Dixon Scott J
Publication year - 2018
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201846666
Subject(s) - palmitoylation , biology , melanocortin , function (biology) , hek 293 cells , biochemistry , serine , microbiology and biotechnology , g protein coupled receptor , enzyme , cysteine , chemistry , receptor
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 ( APT s). 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.