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review article

Mechanisms and functions of protein S-acylation

Mesquita, Francisco S.
•
Abrami, Laurence  
•
Linder, Maurine E.
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February 14, 2024
Nature Reviews Molecular Cell Biology

Over the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator of vital signalling pathways. S-Acylation is a reversible post-translational modification that involves the attachment of a fatty acid to a protein. Maintenance of the equilibrium between protein S-acylation and deacylation has demonstrated profound effects on various cellular processes, including innate immunity, inflammation, glucose metabolism and fat metabolism, as well as on brain and heart function. This Review provides an overview of current understanding of S-acylation and deacylation enzymes, their spatiotemporal regulation by sophisticated multilayered mechanisms, and their influence on protein function, cellular processes and physiological pathways. Furthermore, we examine how disruptions in protein S-acylation are associated with a broad spectrum of diseases from cancer to autoinflammatory disorders and neurological conditions.|Protein S-acylation is involved in many pathophysiological processes. Here, Mesquita et al. discuss the structure, function and regulation of S-acylation and deacylation enzymes and describe how this post-transcriptional modification precisely controls protein-cell membrane interactions. Potential therapeutic applications of S-acylation are also highlighted.

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Type
review article
DOI
10.1038/s41580-024-00700-8
Web of Science ID

WOS:001162195100002

Author(s)
Mesquita, Francisco S.
•
Abrami, Laurence  
•
Linder, Maurine E.
•
Bamji, Shernaz X.
•
Dickinson, Bryan C.
•
van der Goot, F Gisou  
Date Issued

2024-02-14

Publisher

Nature Portfolio

Published in
Nature Reviews Molecular Cell Biology
Subjects

Life Sciences & Biomedicine

•

Ankyrin-Repeat Domain

•

Cysteine-Rich Domain

•

Dynamic Palmitoylation

•

Substrate Recognition

•

Crystal-Structure

•

Hydrolase Domain

•

Plasma-Membrane

•

Molecular-Basis

•

Dhhc Proteins

•

Gasdermin D

Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
VDG  
FunderGrant Number

Swiss National Science Foundation

SNSF-31CA30_196651

Carigest SA

National Institute of General Medical Sciences of the National Institutes of Health (NIH)

R35 GM119840

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Available on Infoscience
March 18, 2024
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/206391
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