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Palmitoylation and depalmitoylation defects

Hornemann, Thorsten

In: Journal of Inherited Metabolic Disease, 2015, vol. 38, no. 1, p. 179-186

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    Title
    • Palmitoylation and depalmitoylation defects
    Author
    • Hornemann, Thorsten. Institute for Clinical Chemistry, University Hospital Zurich, Raemistrasse 100, CH-8091, Zurich, Switzerland
    Document Type
    • Postprint
    Language
    • English
    Published in
    • Journal of Inherited Metabolic Disease, 2015, vol. 38, no. 1, p. 179-186. Springer Netherlands
    Other Version
    Classification
    • Health
    OAI-PMH Identifier
    • oai:doc.rero.ch:332382
    Summary
    Palmitoylation describes the enzymatic attachment of a 16-carbon atom fatty acid to a target protein. Such lipidation events occur in all eukaryotes and can be of reversible (S-palmitoylation) or irreversible (N-palmitoylation) nature. In particular S-palmitoylation is dynamically regulated by two opposing types of enzymes which add (palmitoyl acyltransferases - PAT) or remove (acyl protein thioesterases) palmitate from proteins. Protein palmitoylation is an important process that dynamically regulates the assembly and compartmentalization of many neuronal proteins at specific subcellular sites. Enzymes that regulate protein palmitoylation are critical for several biological processes. To date, eight palmitoylation related genes have been reported to be associated with human disease. This review intends to give an overview on the pathological changes which are associated with defects in the palmitoylation/depalmitoylation process.