Regulatory effects of protein S-acylation on insulin secretion and insulin action

Luke H. Chamberlain, Michael J. Shipston, Gwyn W. Gould

Research output: Contribution to journalReview articlepeer-review

3 Citations (Scopus)
27 Downloads (Pure)


Post-translational modifications (PTMs) such as phosphorylation and ubiquitination are well-studied events with a recognized importance in all aspects of cellular function. By contrast, protein S-acylation, although a widespread PTM with important functions in most physiological systems, has received far less attention. Perturbations in S-acylation are linked to various disorders, including intellectual disability, cancer and diabetes, suggesting that this less-studied modification is likely to be of considerable biological importance. As an exemplar, in this review, we focus on the newly emerging links between S-acylation and the hormone insulin. Specifically, we examine how S-acylation regulates key components of the insulin secretion and insulin response pathways. The proteins discussed highlight the diverse array of proteins that are modified by S-acylation, including channels, transporters, receptors and trafficking proteins and also illustrate the diverse effects that S-acylation has on these proteins, from membrane binding and micro-localization to regulation of protein sorting and protein interactions.

Original languageEnglish
Article number210017
Number of pages16
JournalOpen Biology
Issue number3
Early online date31 Mar 2021
Publication statusPublished - 31 Mar 2021


  • S-acylation
  • zDHHC enzymes
  • acyl protein thioesterase
  • insulin secretion
  • insulin signalling
  • GLUT4


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