title: The intracellular dynamic of protein palmitoylation.
abstract: S-palmitoylation describes the reversible attachment of fatty acids (predominantly palmitate) onto cysteine residues via a labile thioester bond. This posttranslational modification impacts protein functionality by regulating membrane interactions, intracellular sorting, stability, and membrane micropatterning. Several recent findings have provided a tantalizing insight into the regulation and spatiotemporal dynamics of protein palmitoylation. In mammalian cells, the Golgi has emerged as a possible super-reaction center for the palmitoylation of peripheral membrane proteins, whereas palmitoylation reactions on post-Golgi compartments contribute to the regulation of specific substrates. In addition to palmitoylating and depalmitoylating enzymes, intracellular palmitoylation dynamics may also be controlled through interplay with distinct posttranslational modifications, such as phosphorylation and nitrosylation.
authors.affiliation: Institut National de la Santé et de la Recherche Médicale U845, Faculte de Medecine Paris Descartes, 75730 Paris, Cedex 15, France.
authors.forename: Christine
authors.initials: C
authors.lastname: Salaun
authors.forename: Jennifer
authors.initials: J
authors.lastname: Greaves
authors.forename: Luke H
authors.initials: LH
authors.lastname: Chamberlain
mesh_terms: D000818:Animals; D006056:Golgi Apparatus / Q000378:metabolism; D006801:Humans; D054878:Lipoylation / Q000502:physiology*; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D021381:Protein Transport / Q000502:physiology