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

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 receive...

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Bibliographic Details
Published in:Open biology 2021-03, Vol.11 (3), p.210017
Main Authors: Chamberlain, Luke H, Shipston, Michael J, Gould, Gwyn W
Format: Article
Language:English
Subjects:
acyl protein thioesterase
Acylation
Animals
glut4
Humans
Insulin - metabolism
Insulin Secretion
insulin signalling
Protein Processing, Post-Translational
Review
s-acylation
Signal Transduction
zdhhc enzymes
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Summary: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.
ISSN:2046-2441
2046-2441
DOI:10.1098/rsob.210017