The intracellular dynamic of protein palmitoylation

Christine Salaun, Jennifer Greaves, Luke H Chamberlain

Research output: Contribution to journalArticle

172 Citations (Scopus)

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.
LanguageEnglish
Pages1229-1238
Number of pages10
JournalJournal of Cell Biology
Volume191
Issue number7
DOIs
Publication statusPublished - 27 Dec 2010

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Lipoylation
Post Translational Protein Processing
Proteins
Intracellular Membranes
Palmitates
Cysteine
Membrane Proteins
Fatty Acids
Phosphorylation
Membranes
Enzymes

Keywords

  • animals
  • golgi apparatus
  • humans
  • lipoylation
  • protein processing
  • protein transport

Cite this

Salaun, Christine ; Greaves, Jennifer ; Chamberlain, Luke H. / The intracellular dynamic of protein palmitoylation. In: Journal of Cell Biology. 2010 ; Vol. 191, No. 7. pp. 1229-1238.
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The intracellular dynamic of protein palmitoylation. / Salaun, Christine; Greaves, Jennifer; Chamberlain, Luke H.

In: Journal of Cell Biology, Vol. 191, No. 7, 27.12.2010, p. 1229-1238.

Research output: Contribution to journalArticle

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