Salaun, Christine and Greaves, Jennifer and Chamberlain, Luke H (2010) The intracellular dynamic of protein palmitoylation. Journal of Cell Biology, 191 (7). pp. 1229-1238.Full text not available in this repository. (Request a copy from the Strathclyde author)
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.
|Keywords:||animals, golgi apparatus, humans, lipoylation, protein processing, protein transport, Therapeutics. Pharmacology, Cell Biology|
|Subjects:||Medicine > Therapeutics. Pharmacology|
|Department:||Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences|
|Depositing user:||Pure Administrator|
|Date Deposited:||10 Aug 2011 09:08|
|Last modified:||24 Mar 2017 06:16|