Historical Background
Protein palmitoylation is the first discovered and the most common lipid modification. This posttranslational change involves addition of the saturated 16-carbon palmitate to specific cysteine residues by a labile thioester linkage (Linder and Deschenes 2007). Although reversible palmitoylation was discovered over 30 years ago, the enzymes that add palmitate to proteins (palmitoyl acyl transferases, PATs) and those that cleave the thioester bond (palmitoyl protein thioesterases, PPTs) had been elusive. In 2002, genetic screening in yeast identified proteins that mediate PAT activity. Erf2/4 (Lobo et al. 2002) and Akr1 (Roth et al. 2002) were identified as PATs for yeast Ras2 and Yck2, respectively. Erf2 and Akr1 share a conserved DHHC (Asp-His-His-Cys) cysteine-rich domain (CRD) (Fig. 1) and have four or six transmembrane domains. The DHHC sequence and its surrounding CRD sequence...
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Oku, S., Fukata, Y., Fukata, M. (2012). DHHC Proteins. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-0461-4_322
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DOI: https://doi.org/10.1007/978-1-4419-0461-4_322
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