Regulation of T cell function by protein S-acylation [PDF]
Frontiers in Physiology, 2022 S-acylation, the reversible lipidation of free cysteine residues with long-chain fatty acids, is a highly dynamic post-translational protein modification that has recently emerged as an important regulator of the T cell function. The reversible nature of
Savannah J. West +4 more
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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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Regulation of Dynamic Protein S-Acylation [PDF]
Frontiers in Molecular Biosciences, 2021 Protein S-acylation is the reversible addition of fatty acids to the cysteine residues of target proteins. It regulates multiple aspects of protein function, including the localization to membranes, intracellular trafficking, protein interactions ...
Jessica J. Chen +2 more
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Regulatory effects of protein S-acylation on insulin secretion and insulin action [PDF]
Open Biology, 2021 Post-translational modifications (PTMs) such as phosphorylation and ubiquitination are well-studied events with a recognized importance in all aspects of cellular function.
Luke H. Chamberlain +2 more
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Global, site-specific analysis of neuronal protein S-acylation [PDF]
Scientific Reports, 2017 Protein S-acylation (palmitoylation) is a reversible lipid modification that is an important regulator of dynamic membrane-protein interactions. Proteomic approaches have uncovered many putative palmitoylated proteins however, methods for comprehensive ...
Mark O. Collins +2 more
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The landscape of renal protein S-acylation in mice with lipid-induced nephrotoxicity [PDF]
Scientific ReportsExcess fat intake is associated with kidney toxicity and dysfunction. Because fatty acids can also be reversibly attached onto cysteine residues and modulate the function of several membrane-bound proteins, we studied the effect of high-fat diet (HFD) on
Fangrui Xiu +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 protein S-acylation in vascular injury associated with metabolic disorders [PDF]
Frontiers in EndocrinologyProtein palmitoylation represents a prevalent form post-translational lipid modification across various organisms. This reversible and dynamic cellular process is significant in regulating the transcription and expression of downstream target genes, as ...
Yayun Wang +8 more
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Dynamic Protein S-Acylation in Plants [PDF]
International Journal of Molecular Sciences, 2019 Lipid modification is an important post-translational modification. S-acylation is unique among lipid modifications, as it is reversible and has thus attracted much attention. We summarize some proteins that have been shown experimentally to be S-acylated in plants. Two of these S-acylated proteins have been matched to the S-acyl transferase.
Wang Tao, Jiangli Dong, Qianwen Liu
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Proteomic analysis of a poplar cell suspension culture suggests a major role of protein S-acylation in diverse cellular processes [PDF]
Frontiers in Plant Science, 2016 S-acylation is a reversible post-translational modification (PTM) of proteins known to be involved in membrane targeting, subcellular trafficking and the determination of a great variety of functional properties of proteins.
Vaibhav eSrivastava +5 more
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