ABSTRACT
Almost two decades have passed since seminal work in Saccharomyces cerevisiae identified zinc finger DHHC domain-containing (zDHHC) enzymes as S-acyltransferases. These enzymes are ubiquitous in the eukarya domain, with 23 distinct zDHHC-encoding genes in the human genome. zDHHC enzymes mediate the bulk of S-acylation (also known as palmitoylation) reactions in cells, transferring acyl chains to cysteine thiolates, and in so-doing affecting the stability, localisation and function of several thousand proteins. Studies using purified components have shown that the minimal requirements for S-acylation are an appropriate zDHHC enzyme–substrate pair and fatty acyl-CoA. However, additional proteins including GCP16 (also known as Golga7), Golga7b, huntingtin and selenoprotein K, have been suggested to regulate the activity, stability and trafficking of certain zDHHC enzymes. In this Review, we discuss the role of these accessory proteins as essential components of the cellular S-acylation system.
Footnotes
Competing interests
The authors declare no competing or financial interests.
Funding
Work in the authors’ laboratory is funded by the Biotechnology and Biological Sciences Research Council (BBSRC; BB/L022087/1 to L.H.C.) and the Medical Research Council (MRC; MR/R011842/1 and MR/S011080/1 to L.H.C.). We are grateful to the University of Strathclyde for stipend and fee support for the studentship of C.L.
Supplementary information
Supplementary information available online at https://jcs.biologists.org/lookup/doi/10.1242/jcs.251819.supplemental
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