Structure and function of DHHC protein S-acyltransferases

Biochem Soc Trans. 2017 Aug 15;45(4):923-8. doi: 10.1042/BST20160304. Epub 2017 Jun 19.


It has been estimated that 10% of the human genome encodes proteins that are fatty acylated at cysteine residues. The vast majority of these proteins are modified by members of the DHHC protein family, which carry out their enzymatic function on the cytoplasmic face of cell membranes. The biomedical importance of DHHC proteins is underscored by their association with human disease; unique and essential roles for DHHC proteins have been uncovered using DHHC-deficient mouse models. Accordingly, there is great interest in elucidating the molecular mechanisms that underlie DHHC protein function. In this review, we present recent insights into the structure and function of DHHC enzymes.

Keywords: palmitoylation; post-translational modification; protein acyltransferase.

Publication types

  • Review

MeSH terms

  • Acyltransferases / chemistry
  • Acyltransferases / genetics
  • Acyltransferases / metabolism*
  • Animals
  • Cysteine / metabolism*
  • Humans
  • Isoenzymes / chemistry
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Lipoylation
  • Mutation
  • Palmitic Acid
  • Protein Conformation
  • Protein Interaction Domains and Motifs
  • Protein Processing, Post-Translational*
  • Species Specificity
  • Substrate Specificity


  • Isoenzymes
  • Palmitic Acid
  • Acyltransferases
  • Cysteine