Journal of Inherited Metabolic Disease

, Volume 38, Issue 1, pp 179–186 | Cite as

Palmitoylation and depalmitoylation defects

  • Thorsten HornemannEmail author
Complex Lipids


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.


Amyloid Precursor Protein Palmitoyl Neuronal Ceroid Lipofuscinosis Batten Disease YAC128 Mouse 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.



T. Hornemann is grateful to the Gebert Rüf Foundation (GRS-047/09), the Center of Integrated Human Physiology (ZIHP) and “radiz” – Rare Disease Initiative Zurich, Clinical Research Priority Program for Rare Diseases, University of Zurich.

Compliance with ethics guidelines

This article does not contain any studies with human or animal subjects performed by the author.

Conflict of interest



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© SSIEM 2014

Authors and Affiliations

  1. 1.Institute for Clinical ChemistryUniversity Hospital ZurichZurichSwitzerland
  2. 2.Institute of Physiology and Zurich Center for Integrative Human Physiology (ZIHP)University of ZurichZurichSwitzerland

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