Abstract
Palmitoylation (S-acylation) is the posttranslational attachment of fatty acids to cysteine residues and is common among integral and peripheral-membrane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells. Integral membrane proteins are palmitoylated at cysteine residues located at the boundary between the transmembrane segment and the cytoplasmic tail. Peripheral membrane proteins are often acylated at a N-terminal MGCXXS motif, which provides a dual signal for amide-myristoylation, as well as S-palmitoylation. However, comparison of the amino acids in the vicinity of all known palmitoylated cysteine residues reveals no obvious consensus signal for palmitoylation. Thus, palmitoylation of a protein cannot be predicted from its amino acid sequence. An enzyme responsible for the transfer of fatty acids (PAT) has not yet been purified, but several in vitro systems suggest that it is membrane-bound (1–5).
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Veit, M., Schmidt, M.F.G. (1998). Membrane Targeting via Protein Palmitoylation. In: Clegg, R.A. (eds) Protein Targeting Protocols. Methods in Molecular Biology™, vol 88. Humana Press. https://doi.org/10.1385/0-89603-487-9:227
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DOI: https://doi.org/10.1385/0-89603-487-9:227
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