S-acylation of P2K1 mediates extracellular ATP-induced immune signaling in Arabidopsis
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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Site-specific analysis of protein S-acylation by resin-assisted capture[S]
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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2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities. [PDF]
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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Open Biology: overview for special issue on dynamics of protein fatty acylation
Fatty acylation is a widespread form of protein modification that occurs on specific intracellular and secreted proteins. Beyond increasing hydrophobicity and the affinity of the modified protein for lipid bilayers, covalent attachment of a fatty acid ...
Marilyn D. Resh
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The Physiology of ProteinS-acylation [PDF]
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 ...
Chamberlain, Luke H. +1 more
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In vitro reconstitution of substrate S-acylation by the zDHHC family of protein acyltransferases
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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AbstractProteins can be acylated with a variety of fatty acids attached by different covalent bonds, influencing, among other things, their function and intracellular localization. This unit describes methods to analyze protein acylation, both levels of acylation and also the identification of the fatty acid and the type of bond present in the protein ...
Zeidman, R, Jackson, CS, Magee, AI
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Research Progress on Acylation Modification and Application of Animal and Vegetable Proteins [PDF]
Acylation is a common method for chemical modification of proteins, which can effectively improve the functional properties of proteins and has been widely used in food processing in recent years.
YAO Xuan, LÜ Xiaohui, JIN Yongguo, HU Gan
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Distinct Roles of N-Terminal Fatty Acid Acylation of the Salinity-Sensor Protein SOS3
The Salt-Overly-Sensitive (SOS) pathway controls the net uptake of sodium by roots and the xylematic transfer to shoots in vascular plants. SOS3/CBL4 is a core component of the SOS pathway that senses calcium signaling of salinity stress to activate and ...
Irene Villalta +10 more
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Acyl–Acyl Carrier Protein Desaturases and Plant Biotic Interactions [PDF]
Interactions between land plants and other organisms such as pathogens, pollinators, or symbionts usually involve a variety of specialized effectors participating in complex cross-talks between organisms. Fatty acids and their lipid derivatives play important roles in these biological interactions. While the transcriptional regulation of genes encoding
Sami Kazaz +2 more
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