Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications. [PDF]
J Cell Biol, 2023 With a limited number of genes, cells achieve remarkable diversity. This is to a large extent achieved by chemical posttranslational modifications of proteins. Amongst these are the lipid modifications that have the unique ability to confer hydrophobicity.
Anwar MU, van der Goot FG.
europepmc +5 more sources
Regulation of ERK2 activity by dynamic S-acylation [PDF]
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
doaj +2 more sources
Protein S-acyltransferases and acyl protein thioesterases, regulation executors of protein S-acylation in plants [PDF]
Frontiers in Plant Science, 2022 Protein S-acylation, also known as palmitoylation, is an important lipid post-translational modification of proteins in eukaryotes. S-acylation plays critical roles in a variety of protein functions involved in plant development and responses to abiotic ...
Jincheng Li, Manqi Zhang, Lijuan Zhou
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Sequestering sequestosome 1 via S-acylation in autophagy, Huntington disease, and beyond [PDF]
Autophagy ReportsProtein mislocalization and aggregation are hallmark features in neurodegeneration. As proteins mislocalize, proteostasis deficiency and protein aggregation typically follow.
Y Alshehabi, F Abrar, D.D.O Martin
doaj +2 more sources
FASN inhibitor TVB-3166 prevents S-acylation of the spike protein of human coronaviruses [PDF]
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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Site-specific analysis of protein S-acylation by resin-assisted capture[S] [PDF]
Journal of Lipid Research, 2011 Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain ...
Michael T. Forrester +6 more
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S-acylation of P2K1 mediates extracellular ATP-induced immune signaling in Arabidopsis [PDF]
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
doaj +2 more sources
S-acylation of NLRP3 provides a nigericin sensitive gating mechanism that controls access to the Golgi [PDF]
eLifeNLRP3 is an inflammasome seeding pattern recognition receptor activated in response to multiple danger signals which perturb intracellular homeostasis.
Daniel M Williams, Andrew A Peden
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In vitro reconstitution of substrate S-acylation by the zDHHC family of protein acyltransferases [PDF]
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
doaj +2 more sources
The physiology of protein S-acylation [PDF]
Physiological Reviews, 2015 Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes.
Chamberlain, Luke H. +1 more
core +6 more sources