S-acylation is a reversible lipid modification occurring on cysteine residues mediated by a family of membrane-bound ‘zDHHC’ enzymes. S-acylation predominantly results in anchoring of soluble proteins to membrane compartments or in the trafficking of membrane proteins to different compartments. Recent work has shown that although S-acylation of some proteins may involve very weak interactions with zDHHC enzymes, a pool of zDHHC enzymes exhibit strong and specific interactions with substrates, thereby recruiting them for S-acylation. For example, the ankyrin-repeat domains of zDHHC17 and zDHHC13 interact specifically with unstructured consensus sequences present in some proteins, thus contributing to substrate specificity of these enzymes. In addition to this new information on zDHHC enzyme protein substrate specificity, recent work has also identified marked differences in selectivity of zDHHC enzymes for acyl-CoA substrates and has started to unravel the underlying molecular basis for this lipid selectivity. This review will focus on the protein and acyl-CoA selectivity of zDHHC enzymes.
Substrate selectivity in the zDHHC family of S-acyltransferases
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Kimon Lemonidis, Christine Salaun, Marianna Kouskou, Cinta Diez-Ardanuy, Luke H. Chamberlain, Jennifer Greaves; Substrate selectivity in the zDHHC family of S-acyltransferases. Biochem Soc Trans 15 June 2017; 45 (3): 751–758. doi: https://doi.org/10.1042/BST20160309
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