Mechanisms and functions of protein S-acylation. [PDF]
Nat Rev Mol Cell BiolOver 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.
S Mesquita F +5 more
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FASN inhibitor TVB-3166 prevents S-acylation of the spike protein of human coronaviruses
Journal of Lipid Research, 2022 The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and other coronaviruses mediates host cell entry and is S-acylated on multiple phylogenetically conserved cysteine residues.
Katrina Mekhail +13 more
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Palmitoylation: a protein S-acylation with implications for breast cancer. [PDF]
NPJ Breast Cancer, 2016 AbstractProtein S-acylation is a reversible post-translational lipid modification that involves linkage of a fatty acid chain predominantly to a cysteine amino acid via a thioester bond. The fatty acid molecule is primarily palmitate, thus the term ‘palmitoylation’ is more commonly used.
Anderson AM, Ragan MA.
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Regulation of ERK2 activity by dynamic S-acylation
Cell Reports, 2023 Summary: Extracellular signal-regulated kinases (ERK1/2) are key effector proteins of the mitogen-activated protein kinase pathway, choreographing essential processes of cellular physiology.
Saara-Anne Azizi +3 more
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S-acylation of P2K1 mediates extracellular ATP-induced immune signaling in Arabidopsis
Nature Communications, 2021 S-acylation is a reversible protein post-translational modification that often regulates protein function at the plasma membrane. Here the authors show that an Arabidopsis extracellular ATP receptor P2K1 mediates phosphorylation of two S-acyltransferases
Dongqin Chen +5 more
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In vitro reconstitution of substrate S-acylation by the zDHHC family of protein acyltransferases
Open Biology, 2022 Protein S-acylation, more commonly known as protein palmitoylation, is a biological process defined by the covalent attachment of long chain fatty acids onto cysteine residues of a protein, effectively altering the local hydrophobicity and influencing ...
R. Elliot Murphy, Anirban Banerjee
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The role of S‐acylation in protein trafficking [PDF]
Traffic, 2017 Protein S‐acylation, also known as palmitoylation, consists of the addition of a lipid molecule to one or more cysteine residues through a thioester bond. This modification, which is widespread in eukaryotes, is thought to affect over 12% of the human proteome.
José L. Daniotti +2 more
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Accessory proteins of the zDHHC family of S-acylation enzymes [PDF]
Journal of Cell Science, 2020 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.
Christine Salaun +4 more
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2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities. [PDF]
PLoS ONE, 2013 S-acylation, the covalent attachment of palmitate and other fatty acids on cysteine residues, is a reversible post-translational modification that exerts diverse effects on protein functions.
Maria P Pedro +5 more
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Juxta-membrane S-acylation of plant receptor-like kinases is likely fortuitous and does not necessarily impact upon function [PDF]
, 2019 This work was funded by UK Biotechnology and Biological Sciences Research Council Grants BB/M024911/1 and BB/M010996/1 to P.A.H.S-acylation is a common post-translational modification of membrane protein cysteine residues with many regulatory roles.
Hemsley, Piers +5 more
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