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Articles de revues sur le sujet « S-Acylation »

Auteur : Grafiati

Publié le 17 mai 2025

Mis à jour le 25 juillet 2025

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1

Chamberlain, Luke H., and Michael J. Shipston. "The Physiology of Protein S-acylation." Physiological Reviews 95, no. 2 (2015): 341–76. http://dx.doi.org/10.1152/physrev.00032.2014.

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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. S-acylation results from the enzymatic addition of long-chain lipids, most typically palmitate, onto intracellular cysteine residues of soluble and transmembrane proteins via a labile thioester linkage. Addition of lipid results in increases in protein hydrophobicity that can impact on protein structure, assembly, maturation, trafficking, and function

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Shipston, Michael J. "Ion channel regulation by protein S-acylation." Journal of General Physiology 143, no. 6 (2014): 659–78. http://dx.doi.org/10.1085/jgp.201411176.

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Protein S-acylation, the reversible covalent fatty-acid modification of cysteine residues, has emerged as a dynamic posttranslational modification (PTM) that controls the diversity, life cycle, and physiological function of numerous ligand- and voltage-gated ion channels. S-acylation is enzymatically mediated by a diverse family of acyltransferases (zDHHCs) and is reversed by acylthioesterases. However, for most ion channels, the dynamics and subcellular localization at which S-acylation and deacylation cycles occur are not known. S-acylation can control the two fundamental determinants of ion

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Hemsley, Piers A. "S-acylation in plants: an expanding field." Biochemical Society Transactions 48, no. 2 (2020): 529–36. http://dx.doi.org/10.1042/bst20190703.

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S-acylation is a common yet poorly understood fatty acid-based post-translational modification of proteins in all eukaryotes, including plants. While exact roles for S-acylation in protein function are largely unknown the reversibility of S-acylation indicates that it is likely able to play a regulatory role. As more studies reveal the roles of S-acylation within the cell it is becoming apparent that how S-acylation affects proteins is conceptually different from other reversible modifications such as phosphorylation or ubiquitination; a new mind-set is therefore required to fully integrate th

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Locatelli, Carolina, Kimon Lemonidis, Christine Salaun, Nicholas C. O. Tomkinson, and Luke H. Chamberlain. "Identification of key features required for efficient S-acylation and plasma membrane targeting of sprouty-2." Journal of Cell Science 133, no. 21 (2020): jcs249664. http://dx.doi.org/10.1242/jcs.249664.

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ABSTRACTSprouty-2 is an important regulator of growth factor signalling and a tumour suppressor protein. The defining feature of this protein is a cysteine-rich domain (CRD) that contains twenty-six cysteine residues and is modified by S-acylation. In this study, we show that the CRD of sprouty-2 is differentially modified by S-acyltransferase enzymes. The high specificity/low activity zDHHC17 enzyme mediated restricted S-acylation of sprouty-2, and cysteine-265 and -268 were identified as key targets of this enzyme. In contrast, the low specificity/high activity zDHHC3 and zDHHC7 enzymes medi

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BAÑÓ, M. Carmen, S. Caroline JACKSON, and I. Anthony MAGEE. "Pseudo-enzymatic S-acylation of a myristoylated Yes protein tyrosine kinase peptide in vitro may reflect non-enzymatic S-acylation in vivo." Biochemical Journal 330, no. 2 (1998): 723–31. http://dx.doi.org/10.1042/bj3300723.

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Covalent attachment of a variety of lipid groups to proteins is now recognized as a major group of post-translational modifications. S-acylation of proteins at cysteine residues is the only modification considered dynamic and thus has the potential for regulating protein function and/or localization. The activities that catalyse reversible S-acylation have not been well characterized and it is not clear whether both the acylation and the deacylation steps are regulated, since in principle it would be sufficient to control only one of them. Both apparently enzymatic and non-enzymatic S-acylatio

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Hines, P. J. "Location, location, S-acylation." Science 353, no. 6295 (2016): 133–34. http://dx.doi.org/10.1126/science.353.6295.133-f.

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Zheng, Lihua, Peng Liu, Qianwen Liu, Tao Wang, and Jiangli Dong. "Dynamic Protein S-Acylation in Plants." International Journal of Molecular Sciences 20, no. 3 (2019): 560. http://dx.doi.org/10.3390/ijms20030560.

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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. More importantly, the first protein thioesterase with de-S-acylation activity has been identified in plants. This review shows that S-acylation is important for a variety of different functions in plants and that there are many unexplored aspects of S-acy

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Lemonidis, Kimon, Oforiwa A. Gorleku, Maria C. Sanchez-Perez, Christopher Grefen, and Luke H. Chamberlain. "The Golgi S-acylation machinery comprises zDHHC enzymes with major differences in substrate affinity and S-acylation activity." Molecular Biology of the Cell 25, no. 24 (2014): 3870–83. http://dx.doi.org/10.1091/mbc.e14-06-1169.

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S-acylation, the attachment of fatty acids onto cysteine residues, regulates protein trafficking and function and is mediated by a family of zDHHC enzymes. The S-acylation of peripheral membrane proteins has been proposed to occur at the Golgi, catalyzed by an S-acylation machinery that displays little substrate specificity. To advance understanding of how S-acylation of peripheral membrane proteins is handled by Golgi zDHHC enzymes, we investigated interactions between a subset of four Golgi zDHHC enzymes and two S-acylated proteins—synaptosomal-associated protein 25 (SNAP25) and cysteine-str

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Zhang, Lian, Karyn Foster, Qiuju Li, and Jeffrey R. Martens. "S-acylation regulates Kv1.5 channel surface expression." American Journal of Physiology-Cell Physiology 293, no. 1 (2007): C152—C161. http://dx.doi.org/10.1152/ajpcell.00480.2006.

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The number of ion channels expressed on the cell surface shapes the complex electrical response of excitable cells. An imbalance in the ratio of inward and outward conducting channels is unfavorable and often detrimental. For example, over- or underexpression of voltage-gated K+ (Kv) channels can be cytotoxic and in some cases lead to disease. In this study, we demonstrated a novel role for S-acylation in Kv1.5 cell surface expression. In transfected fibroblasts, biochemical evidence showed that Kv1.5 is posttranslationally modified on both the NH2 and COOH termini via hydroxylamine-sensitive

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Schroeder, H., R. Leventis, S. Shahinian, P. A. Walton, and J. R. Silvius. "Lipid-modified, cysteinyl-containing peptides of diverse structures are efficiently S-acylated at the plasma membrane of mammalian cells." Journal of Cell Biology 134, no. 3 (1996): 647–60. http://dx.doi.org/10.1083/jcb.134.3.647.

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A variety of cysteine-containing, lipid-modified peptides are found to be S-acylated by cultured mammalian cells. The acylation reaction is highly specific for cysteinyl over serinyl residues and for lipid-modified peptides over hydrophilic peptides. The S-acylation process appears by various criteria to be enzymatic and resembles the S-acylation of plasma membrane-associated proteins in various characteristics, including inhibition by tunicamycin. The substrate range of the S-acylation reaction encompasses, but is not limited to, lipopeptides incorporating the motifs myristoylGC- and -CXC(far

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Manhertz-Patterson, Rojae, and G. Ekin Atilla-Gokcumen. "S-acylation in apoptotic and non-apoptotic cell death: a central regulator of membrane dynamics and protein function." Biochemical Society Transactions 53, no. 02 (2025): 487–96. https://doi.org/10.1042/bst20253012.

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Protein lipidation is a collection of important post-translational modifications that modulate protein localization and stability. Protein lipidation affects protein function by facilitating interactions with cellular membranes, changing the local environment of protein interactions. Among these modifications, S-acylation has emerged as a key regulator of various cellular processes, including different forms of cell death. In this mini-review, we highlight the role of S-acylation in apoptosis and its emerging contributions to necroptosis and pyroptosis. While traditionally associated with the

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Jones, David, Uday Khandavilli, Eileen O’Leary, Simon Lawrence, and Timothy O’Sullivan. "Efficient S-Acylation of Thiourea." SynOpen 02, no. 04 (2018): 0263–67. http://dx.doi.org/10.1055/s-0037-1610370.

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Efficient S-acylation of thiourea using a variety of acid chlorides is reported. Structurally diverse aryl and alkyl substrates are compatible with this methodology. Confirmation that acylation occurs exclusively on the sulfur atom of thiourea is provided by single-crystal X-ray crystallographic analysis.

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Greaves, Jennifer, and Luke H. Chamberlain. "S-acylation by the DHHC protein family." Biochemical Society Transactions 38, no. 2 (2010): 522–24. http://dx.doi.org/10.1042/bst0380522.

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A family of 23 DHHC (Asp-His-His-Cys) proteins that function as mammalian S-acyltransferases has been identified, reinvigorating the study of protein S-acylation. Recent studies have continued to reveal how S-acylation affects target proteins, and have provided glimpses of how DHHC-substrate specificity might be achieved.

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Salaun, Christine, Jennifer Greaves, Nicholas C. O. Tomkinson, and Luke H. Chamberlain. "The linker domain of the SNARE protein SNAP25 acts as a flexible molecular spacer that ensures efficient S-acylation." Journal of Biological Chemistry 295, no. 21 (2020): 7501–15. http://dx.doi.org/10.1074/jbc.ra120.012726.

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S-Acylation of the SNARE protein SNAP25 (synaptosome-associated protein of 25 kDa) is mediated by a subset of Golgi zinc finger DHHC-type palmitoyltransferase (zDHHC) enzymes, particularly zDHHC17. The ankyrin repeat domain of zDHHC17 interacts with a short linear motif known as the zDHHC ankyrin repeat–binding motif (zDABM) in SNAP25 (112VVASQP117), which is downstream of its S-acylated, cysteine-rich domain (85CGLCVCPC92). Here, we investigated the importance of a flexible linker region (amino acids 93–111, referred to hereafter as the “mini-linker” region) that separates the zDABM and S-acy

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Lemonidis, Kimon, Christine Salaun, Marianna Kouskou, Cinta Diez-Ardanuy, Luke H. Chamberlain, and Jennifer Greaves. "Substrate selectivity in the zDHHC family of S-acyltransferases." Biochemical Society Transactions 45, no. 3 (2017): 751–58. http://dx.doi.org/10.1042/bst20160309.

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S-acylation is a reversible lipid modification occurring on cysteine residues mediated by a family of membrane-bound ‘zDHHC’ enzymes. S-acylation predominantly results in anchoring of soluble proteins to membrane compartments or in the trafficking of membrane proteins to different compartments. Recent work has shown that although S-acylation of some proteins may involve very weak interactions with zDHHC enzymes, a pool of zDHHC enzymes exhibit strong and specific interactions with substrates, thereby recruiting them for S-acylation. For example, the ankyrin-repeat domains of zDHHC17 and zDHHC1

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Kordyukova, Larisa V., Marina V. Serebryakova, Vladislav V. Khrustalev, and Michael Veit. "Differential S-acylation of Enveloped Viruses." Protein & Peptide Letters 26, no. 8 (2019): 588–600. http://dx.doi.org/10.2174/0929866526666190603082521.

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Post-translational modifications often regulate protein functioning. Covalent attachment of long chain fatty acids to cysteine residues via a thioester linkage (known as protein palmitoylation or S-acylation) affects protein trafficking, protein-protein and protein-membrane interactions. This post-translational modification is coupled to membrane fusion or virus assembly and may affect viral replication in vitro and thus also virus pathogenesis in vivo. In this review we outline modern methods to study S-acylation of viral proteins and to characterize palmitoylproteomes of virus infected cells

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Hemsley, Piers A. "Protein S-acylation in plants (Review)." Molecular Membrane Biology 26, no. 1-2 (2009): 114–25. http://dx.doi.org/10.1080/09687680802680090.

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Randall, Matthew J., Jennifer L. Ather, Laura R. Hoyt, Anne E. Dixon, and Matthew E. Poynter. "Protein S-Acylation in Pulmonary Disease." Free Radical Biology and Medicine 100 (November 2016): S193. http://dx.doi.org/10.1016/j.freeradbiomed.2016.10.528.

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Percher, Avital, Srinivasan Ramakrishnan, Emmanuelle Thinon, Xiaoqiu Yuan, Jacob S. Yount, and Howard C. Hang. "Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation." Proceedings of the National Academy of Sciences 113, no. 16 (2016): 4302–7. http://dx.doi.org/10.1073/pnas.1602244113.

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Fatty acylation of cysteine residues provides spatial and temporal control of protein function in cells and regulates important biological pathways in eukaryotes. Although recent methods have improved the detection and proteomic analysis of cysteine fatty (S-fatty) acylated proteins, understanding how specific sites and quantitative levels of this posttranslational modification modulate cellular pathways are still challenging. To analyze the endogenous levels of protein S-fatty acylation in cells, we developed a mass-tag labeling method based on hydroxylamine-sensitivity of thioesters and sele

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Pedro, Maria P., Aldo A. Vilcaes, Guillermo A. Gomez, and Jose L. Daniotti. "Individual S-acylated cysteines differentially contribute to H-Ras endomembrane trafficking and acylation/deacylation cycles." Molecular Biology of the Cell 28, no. 7 (2017): 962–74. http://dx.doi.org/10.1091/mbc.e16-08-0603.

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S-acylation/deacylation cycles and vesicular transport are critical for an adequate subcellular distribution of S-acylated Ras proteins. H-Ras is dually acylated on cysteines 181 and 184, but it is unknown how these residues individually contribute to H-Ras trafficking. In this study, we characterized the acylation and deacylation rates and membrane trafficking of monoacylated H-Ras mutants to analyze their contributions to H-Ras plasma membrane and endomembrane distribution. We demonstrated that dually acylated H-Ras interacts with acyl-protein thioesterases (APTs) 1 and 2 at the plasma membr

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Gu, Si, Xinghua Nie, Amal George, et al. "Bioinformatics and Expression Profiling of the DHHC-CRD S-Acyltransferases Reveal Their Roles in Growth and Stress Response in Woodland Strawberry (Fragaria vesca)." Plants 14, no. 1 (2025): 127. https://doi.org/10.3390/plants14010127.

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Protein S-acyl transferases (PATs) are a family of enzymes that catalyze protein S-acylation, a post-translational lipid modification involved in protein membrane targeting, trafficking, stability, and protein–protein interaction. S-acylation plays important roles in plant growth, development, and stress responses. Here, we report the genome-wide analysis of the PAT family genes in the woodland strawberry (Fragaria vesca), a model plant for studying the economically important Rosaceae family. In total, 21 ‘Asp-His-His-Cys’ Cys Rich Domain (DHHC-CRD)-containing sequences were identified, named

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Rana, Mitra S., Chul-Jin Lee, and Anirban Banerjee. "The molecular mechanism of DHHC protein acyltransferases." Biochemical Society Transactions 47, no. 1 (2018): 157–67. http://dx.doi.org/10.1042/bst20180429.

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Abstract Protein S-acylation is a reversible lipidic posttranslational modification where a fatty acid chain is covalently linked to cysteine residues by a thioester linkage. A family of integral membrane enzymes known as DHHC protein acyltransferases (DHHC-PATs) catalyze this reaction. With the rapid development of the techniques used for identifying lipidated proteins, the repertoire of S-acylated proteins continues to increase. This, in turn, highlights the important roles that S-acylation plays in human physiology and disease. Recently, the first molecular structures of DHHC-PATs were dete

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Ticho, Alexander L., Pooja Malhotra, Christopher R. Manzella, et al. "S-acylation modulates the function of the apical sodium-dependent bile acid transporter in human cells." Journal of Biological Chemistry 295, no. 14 (2020): 4488–97. http://dx.doi.org/10.1074/jbc.ra119.011032.

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The ileal apical sodium-dependent bile acid transporter (ASBT) is crucial for the enterohepatic circulation of bile acids. ASBT function is rapidly regulated by several posttranslational modifications. One reversible posttranslational modification is S-acylation, involving the covalent attachment of fatty acids to cysteine residues in proteins. However, whether S-acylation affects ASBT function and membrane expression has not been determined. Using the acyl resin-assisted capture method, we found that the majority of ASBT (∼80%) was S-acylated in ileal brush border membrane vesicles from human

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Zmuda, Filip, and Luke H. Chamberlain. "Regulatory effects of post-translational modifications on zDHHC S-acyltransferases." Journal of Biological Chemistry 295, no. 43 (2020): 14640–52. http://dx.doi.org/10.1074/jbc.rev120.014717.

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The human zDHHC S-acyltransferase family comprises 23 enzymes that mediate the S-acylation of a multitude of cellular proteins, including channels, receptors, transporters, signaling molecules, scaffolds, and chaperones. This reversible post-transitional modification (PTM) involves the attachment of a fatty acyl chain, usually derived from palmitoyl-CoA, to specific cysteine residues on target proteins, which affects their stability, localization, and function. These outcomes are essential to control many processes, including synaptic transmission and plasticity, cell growth and differentiatio

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Salaun, Christine, Carolina Locatelli, Filip Zmuda, Juan Cabrera González, and Luke H. Chamberlain. "Accessory proteins of the zDHHC family of S-acylation enzymes." Journal of Cell Science 133, no. 22 (2020): jcs251819. http://dx.doi.org/10.1242/jcs.251819.

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ABSTRACTAlmost 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. zDHHC enzymes mediate the bulk of S-acylation (also known as palmitoylation) reactions in cells, transferring acyl chains to cysteine thiolates, and in so-doing affecting the stability, localisation and function of several thousand proteins. Studies using purified components have shown that the minimal requirements f

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Mahajan, Dinesh, Varun Kumar, Anil Rana, Chhuttan Lal Meena, Nidhi Sharma, and Yashwant Kumar. "Electrophilic Activation of Carboxylic Anhydrides for Nucleophilic Acylation Reactions." Synthesis 50, no. 19 (2018): 3902–10. http://dx.doi.org/10.1055/s-0037-1609564.

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Nucleophilic acylation of symmetrical carboxylic anhydrides has inherited limitation of reaction efficiency along with relatively poor reactivity. Traditionally, one equivalent carboxylic acid is generated during nucleophilic acylation of a symmetrical anhydride, which always limits the yield of final product to 50% or less. This is a major drawback, which discourages the use of anhydrides for laboratory or industrial applications. Electrophilic activation of carboxylic anhydride using methanesulfonyl chloride is found to be an efficient method for nucleophilic acylation, which increases produ

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West, Savannah J., Goutham Kodakandla, Qiaochu Wang, et al. "S-Acylation regulates store-operated calcium entry." Biophysical Journal 121, no. 3 (2022): 387a. http://dx.doi.org/10.1016/j.bpj.2021.11.828.

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Birner-Gruenberger, Ruth, and Rolf Breinbauer. "Tracking Protein S-Fatty Acylation with Proteomics." ChemBioChem 17, no. 16 (2016): 1488–90. http://dx.doi.org/10.1002/cbic.201600314.

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Motion, R. L., P. D. Buckley, A. F. Bennett, and L. F. Blackwell. "Evidence that the cytoplasmic aldehyde dehydrogenase-catalysed oxidation of aldehydes involves a different active-site group from that which catalyses the hydrolysis of 4-nitrophenyl acetate." Biochemical Journal 254, no. 3 (1988): 903–6. http://dx.doi.org/10.1042/bj2540903.

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Acylation of the aldehyde dehydrogenase. NADH complex by acetic anhydride leads to the production of acetaldehyde and NAD+. By monitoring changes in nucleotide fluorescence, the rate constant for acylation of the active site of the *enzyme. NADH complex was found to be 11 +/- 3 s-1. The rate of acylation by acetic anhydride at the group that binds aldehydes on the oxidative pathway is clearly rapid enough to maintain significant steady-state concentrations of the required active-site-acylated *enzyme. NADH intermediate despite the rapid hydrolysis of this *enzyme.acyl. NADH intermediate (5-10

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Chumpen Ramirez, Sabrina, Fernando M. Ruggiero, Jose Luis Daniotti, and Javier Valdez Taubas. "Ganglioside glycosyltransferases are S-acylated at conserved cysteine residues involved in homodimerisation." Biochemical Journal 474, no. 16 (2017): 2803–16. http://dx.doi.org/10.1042/bcj20170124.

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Ganglioside glycosyltransferases (GGTs) are type II membrane proteins bearing a short N-terminal cytoplasmic tail, a transmembrane domain (TMD), and a lumenal catalytic domain. The expression and activity of these enzymes largely determine the quality of the glycolipids that decorate mammalian cell membranes. Many glycosyltransferases (GTs) are themselves glycosylated, and this is important for their proper localisation, but few if any other post-translational modifications of these proteins have been reported. Here, we show that the GGTs, ST3Gal-V, ST8Sia-I, and β4GalNAcT-I are S-acylated at

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Qiu, Tian, Saara-Anne Azizi, Shubhashree Pani, and Bryan C. Dickinson. "Abstract 1506: Protein acyl-protein thioesterases affect redox homeostasis and ROS signaling through peroxiredoxin." Cancer Research 85, no. 8_Supplement_1 (2025): 1506. https://doi.org/10.1158/1538-7445.am2025-1506.

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Peroxiredoxins (PRDXs) are among the most abundant antioxidants and are widely distributed in cancers. They are associated with tumor cell resistance to cell death, such as apoptosis and ferroptosis. Post-translational modifications of PRDX play a critical role in modulating its activity and tuning the balance between reactive oxygen species (ROS) signaling and stress. We previously discovered that mitochondrial localized PRDX3 and PRDX5 are S-acylated, with dynamic PRDX5 active site cysteine acylation regulating mitochondrial redox homeostasis. In this investigation, we found that all the PRD

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Ghosh, Santanu, Anisha Purkait, and Chandan K. Jana. "Environmentally benign decarboxylative N-, O-, and S-acetylations and acylations." Green Chemistry 22, no. 24 (2020): 8721–27. http://dx.doi.org/10.1039/d0gc03731a.

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Daniotti, Jose L., Maria P. Pedro, and Javier Valdez Taubas. "The role of S-acylation in protein trafficking." Traffic 18, no. 11 (2017): 699–710. http://dx.doi.org/10.1111/tra.12510.

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West, Savannah J., Qiaochu Wang, Michael X. Zhu, Askar M. Akimzhanov, and Darren Boehning. "Regulation of Orai1/STIM1 Function by S-Acylation." Biophysical Journal 118, no. 3 (2020): 404a. http://dx.doi.org/10.1016/j.bpj.2019.11.2292.

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Azizi, Saara-Anne, Tian Qiu, Noah E. Brookes, and Bryan C. Dickinson. "Regulation of ERK2 activity by dynamic S-acylation." Cell Reports 42, no. 9 (2023): 113135. http://dx.doi.org/10.1016/j.celrep.2023.113135.

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Zlatkine, P., B. Mehul, and A. I. Magee. "Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif." Journal of Cell Science 110, no. 5 (1997): 673–79. http://dx.doi.org/10.1242/jcs.110.5.673.

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Several members of the Src family of protein tyrosine kinases have a N-terminal dual acylation motif which specifies their myristoylation and S-acylation. These lipid modifications are necessary for correct intracellular localisation to the plasma membrane and to detergent-resistant glycolipid-enriched membrane domains (GEMs). Using chimaeras of the Lck dual acylation motif with two normally cytosolic proteins (chloramphenicol acetyl transferase and galectin-3), we show here that this motif is sufficient to encode correct lipid modification and to target these chimaeras to the plasma membrane,

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del Rivero Morfin, Pedro J., and Manu Ben-Johny. "Cutting out the fat: Site-specific deacylation of an ion channel." Journal of Biological Chemistry 295, no. 49 (2020): 16497–98. http://dx.doi.org/10.1074/jbc.h120.016490.

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S-Acylation, a reversible post-translational lipid modification of proteins, controls the properties and function of various proteins, including ion channels. Large conductance Ca2+-activated potassium (BK) channels are S-acylated at two sites that impart distinct functional effects. Whereas the enzymes that attach lipid groups are known, the enzymes mediating lipid removal (i.e. deacylation) are largely unknown. Here, McClafferty et al. identify two enzymes, ABHD17a and ABHD17c, that excise BK channel lipid groups with remarkable precision. These findings lend insights into mechanisms that or

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Vysyaraju, Ravikanth, Hanumantha Rao B., Subramanyeswara Rao I. V., Venkateswarlu J., Prasada Rao K. V. V., and Siddaiah V.*. "A Novel Process for the Preparation of [(R,S)/(S,R)] and [(S,S)/(R,R)] Chroman epoxides, Key Intermediates in the Synthesis of Nebivolol." International Journal of Bioassays 6, no. 06 (2017): 5420. http://dx.doi.org/10.21746/ijbio.2017.06.007.

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A novel, cost effective, scalable process for the preparation of chroman epoxides starting from 4-fluorophenol is described. The highlights of the process are single step O-acylation, fries rearrangement, one pot synthesis of claisen condensation, cyclization, reduction, epoxidation with over all yield of 50.9% [(R,S)/(S,R)]-chroman epoxide-A is 33.9% and [(S,S)/(R,R)]-chroman epoxide-B is 17%.

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Li, Yumeng, Shushu Wang, Yanchi Chen, et al. "Site-specific chemical fatty-acylation for gain-of-function analysis of protein S-palmitoylation in live cells." Chemical Communications 56, no. 89 (2020): 13880–83. http://dx.doi.org/10.1039/d0cc06073a.

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Chen, Baoen, Jixiao Niu, Johannes Kreuzer, et al. "Auto-fatty acylation of transcription factor RFX3 regulates ciliogenesis." Proceedings of the National Academy of Sciences 115, no. 36 (2018): E8403—E8412. http://dx.doi.org/10.1073/pnas.1800949115.

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Defects in cilia have been associated with an expanding human disease spectrum known as ciliopathies. Regulatory Factor X 3 (RFX3) is one of the major transcription factors required for ciliogenesis and cilia functions. In addition, RFX3 regulates pancreatic islet cell differentiation and mature β-cell functions. However, how RFX3 protein is regulated at the posttranslational level remains poorly understood. Using chemical reporters of protein fatty acylation and mass spectrometry analysis, here we show that RFX3 transcriptional activity is regulated by S-fatty acylation at a highly conserved

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BARCLAY, Elaine, Mark O'REILLY та Graeme MILLIGAN. "Activation of an α2A-adrenoceptor–Gαo1 fusion protein dynamically regulates the palmitoylation status of the G protein but not of the receptor". Biochemical Journal 385, № 1 (2004): 197–206. http://dx.doi.org/10.1042/bj20041432.

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Post-translational thio-acylation of a fusion protein between the α2A-adrenoceptor and the α subunit of the G protein Go1 is both dynamic and regulated by agonist binding. Incorporation of [3H]palmitate into the fusion protein was reduced substantially in the presence of the agonist adrenaline. This was dependent on the concentration of adrenaline and correlated with occupancy of the ligand binding site. Both the receptor and G-protein elements of the fusion construct incorporated [3H]palmitate but this occurred more rapidly for the G-protein element and regulation of acylation by the agonist

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Stevenson, F. T., S. L. Bursten, R. M. Locksley, and D. H. Lovett. "Myristyl acylation of the tumor necrosis factor alpha precursor on specific lysine residues." Journal of Experimental Medicine 176, no. 4 (1992): 1053–62. http://dx.doi.org/10.1084/jem.176.4.1053.

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NH2-terminal glycine myristyl acylation is a cotranslational modification that affects both protein localization and function. However, several proteins that lack NH2-terminal glycine residues, including the interleukin 1 (IL-1) precursors, also contain covalently linked myristate. To date, the site(s) of acylation of these proteins has not been determined. During an evaluation of IL-1 acylation, it was observed that [3H]myristate-labeled human monocyte lysates contained a prominent 26-kD myristylated protein, which was identified as the tumor necrosis factor alpha (TNF) precursor protein on t

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Pal, Mohan, and Stephen L. Bearne. "Synthesis of coenzyme A thioesters using methyl acyl phosphates in an aqueous medium." Org. Biomol. Chem. 12, no. 48 (2014): 9760–63. http://dx.doi.org/10.1039/c4ob02079k.

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Lutter, Ferdinand H., Lucie Grokenberger, Maximilian S. Hofmayer, and Paul Knochel. "Cobalt-catalyzed acylation-reactions of (hetero)arylzinc pivalates with thiopyridyl ester derivatives." Chemical Science 10, no. 35 (2019): 8241–45. http://dx.doi.org/10.1039/c9sc01817d.

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Kodakandla, Goutham, and Darren F. Boehning. "S-Acylation of STIM1 regulates store-operated calcium entry." Biophysical Journal 121, no. 3 (2022): 371a—372a. http://dx.doi.org/10.1016/j.bpj.2021.11.906.

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Katritzky, Alan, Mohamed Ibrahim, Siva Panda, Linda Nhon, Ahmed Hamed, and Said El-Feky. "Macrocyclic Peptoids by Selective S-Acylation of Cysteine Esters." Synthesis 45, no. 06 (2013): 767–72. http://dx.doi.org/10.1055/s-0032-1318148.

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Kodakandla, Goutham, Michael X. Zhu, Askar M. Akimzhanov, and Darren F. Boehning. "S-acylation of SARAF regulates store-operated calcium entry." Biophysical Journal 122, no. 3 (2023): 373a—374a. http://dx.doi.org/10.1016/j.bpj.2022.11.2057.

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Sakai, Tatsuya, Reiko Ohuchi, and Masanobu Ohuchi. "Fatty Acids on the A/USSR/77 Influenza Virus Hemagglutinin Facilitate the Transition from Hemifusion to Fusion Pore Formation." Journal of Virology 76, no. 9 (2002): 4603–11. http://dx.doi.org/10.1128/jvi.76.9.4603-4611.2002.

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ABSTRACT Influenza virus hemagglutinin (HA) has three highly conserved acylation sites close to the carboxyl terminus of the HA2 subunit, one in the transmembrane domain and two in the cytoplasmic domain. Each site is modified by palmitic acid through a thioester linkage to cysteine. To elucidate the biological significance of HA acylation, the acylation sites of HA of influenza virus strain A/USSR/77 (H1N1) were changed by site-directed mutagenesis, and the membrane fusion activity of mutant HAs lacking the acylation site(s) was examined quantitatively using transfer assays of lipid (R18) and

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Panina, Irina, Nikolay Krylov, Mohamed Rasheed Gadalla, et al. "Molecular Dynamics of DHHC20 Acyltransferase Suggests Principles of Lipid and Protein Substrate Selectivity." International Journal of Molecular Sciences 23, no. 9 (2022): 5091. http://dx.doi.org/10.3390/ijms23095091.

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Lipid modification of viral proteins with fatty acids of different lengths (S-acylation) is crucial for virus pathogenesis. The reaction is catalyzed by members of the DHHC family and proceeds in two steps: the autoacylation is followed by the acyl chain transfer onto protein substrates. The crystal structure of human DHHC20 (hDHHC20), an enzyme involved in the acylation of S-protein of SARS-CoV-2, revealed that the acyl chain may be inserted into a hydrophobic cavity formed by four transmembrane (TM) α-helices. To test this model, we used molecular dynamics of membrane-embedded hDHHC20 and it

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Sklyarenko, A. V., I. A. Groshkova, I. N. Krestyanova, and S. V. Yarotsky. "Alternative Synthesis of Cefamandole with Biocatalytic Acylation Catalyzed by Immobilized Cephalosporin-Acid Synthetase." Applied Biochemistry and Microbiology 58, no. 3 (2022): 251–60. http://dx.doi.org/10.1134/s0003683822030127.

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Abstract The processes of the biocatalytic acylation of 1-methyl-5-mercapto-1,2,3,4-tetrazolil-7-amino-cephalosporanic acid (7-TMCA) and 7-aminocephalosporanic acid (7-ACA) by methyl ester of mandelic acid (MEMA) were optimized with an immobilized cephalosporin-acid synthetase as the biocatalyst. Under optimized conditions in water-organic medium containing 43% (vol/vol) of ethylene glycol at 30°С with a spontaneous pH gradient in the range of 8.0–6.0, the following yields of biocatalytic transformations were reached: (80.8 ± 1.9)% for 7‑TMCA acylation (at a concentration of 100–120 mМ) result

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