Abstract
The attachment of palmitic acid to the amino acid cysteine via thioester linkage (S-palmitoylation) is a common post-translational modification of eukaryotic proteins. In this review, we discuss the role of palmitoylation as a versatile protein sorting signal, regulating protein trafficking between distinct intracellular compartments and the micro-localization of proteins within membranes. © 2009 Informa UK Ltd.
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Greaves, J., Prescott, G. R., Gorleku, O. A., & Chamberlain, L. H. (2009, January). The fat controller: Roles of palmitoylation in intracellular protein trafficking and targeting to membrane microdomains (Review). Molecular Membrane Biology. https://doi.org/10.1080/09687680802620351
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