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Review
Accessory proteins of the zDHHC family of S-acylation enzymes
Christine Salaun, Carolina Locatelli, Filip Zmuda, Juan Cabrera González, Luke H. Chamberlain
Journal of Cell Science 2020 133: jcs251819 doi: 10.1242/jcs.251819 Published 17 November 2020
Christine Salaun
1Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow G4 0RE, UK
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Carolina Locatelli
1Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow G4 0RE, UK
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Filip Zmuda
1Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow G4 0RE, UK
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Juan Cabrera González
2Fac. de Ciencias Químicas, Universidad Complutense, Avda. Complutense s/n, 28040 Madrid, Spain
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Luke H. Chamberlain
1Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow G4 0RE, UK
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  • For correspondence: luke.chamberlain@strath.ac.uk
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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

  • © 2020. Published by The Company of Biologists Ltd
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Keywords

  • S-acylation
  • Palmitoylation
  • ZDHHC enzyme
  • GCP16
  • Golga7
  • Huntingtin
  • Selenoprotein K

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Review
Accessory proteins of the zDHHC family of S-acylation enzymes
Christine Salaun, Carolina Locatelli, Filip Zmuda, Juan Cabrera González, Luke H. Chamberlain
Journal of Cell Science 2020 133: jcs251819 doi: 10.1242/jcs.251819 Published 17 November 2020
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Review
Accessory proteins of the zDHHC family of S-acylation enzymes
Christine Salaun, Carolina Locatelli, Filip Zmuda, Juan Cabrera González, Luke H. Chamberlain
Journal of Cell Science 2020 133: jcs251819 doi: 10.1242/jcs.251819 Published 17 November 2020

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Article navigation

  • Top
  • Article
    • ABSTRACT
    • Introduction
    • Erf4 and GCP16 – accessory proteins for Erf2 and zDHHC9, respectively
    • Regulation of zDHHC5 by GCP16 and Golga7b
    • Regulation of zDHHC17 by huntingtin
    • Regulation of zDHHC6 by selenoprotein K
    • Conclusions and perspectives
    • Footnotes
    • References
  • Figures & tables
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