Results 21 to 30 of about 36,153 (123)
Dynamic Protein S-Acylation in Plants [PDF]
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.
Lihua Zheng +4 more
openaire +2 more sources
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
doaj +1 more source
Salicylic acid attenuates brassinosteroid signaling via protein de-S-acylation. [PDF]
AbstractBrassinosteroids (BRs) are important plant hormones involved in many aspects of development. Here, we show that BRASSINOSTEROID SIGNALING KINASEs (BSKs), key components of the BR pathway, are precisely controlled via de‐S‐acylation mediated by the defense hormone salicylic acid (SA). Most Arabidopsis BSK members are substrates of S‐acylation, a
Liu X +10 more
europepmc +3 more sources
Palmitoylation: A Fatty Regulator of Myocardial Electrophysiology
Regulation of cardiac physiology is well known to occur through the action of kinases that reversibly phosphorylate ion channels, calcium handling machinery, and signaling effectors.
Kobina Essandoh +5 more
doaj +1 more source
Efficient immune responses require Ca2+ fluxes across ORAI1 channels during engagement of T cell receptors (TCR) at the immune synapse (IS) between T cells and antigen presenting cells. Here, we show that ZDHHC20-mediated S-acylation of the ORAI1 channel
Amado Carreras-Sureda +8 more
doaj +1 more source
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
doaj +1 more source
S-Acyl Glutathione Thioesterase of Plant Tissue [PDF]
The enzymic hydrolysis of S-acyl glutathione has been observed in extracts of various plant tissues. The richest source found in this study was avocado mesocarp. No enzymic activity was observed with acetyl coenzyme A or acetylthiocholine as substrates. Hydrolytic activity was essentially constant in the pH range 7 to 9.
L K, Winberry, J B, Mudd
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Assaying protein palmitoylation in plants
Background Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes.
Taylor Laura +2 more
doaj +1 more source
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
doaj +1 more source
Dynamic PRDX S-acylation modulates ROS stress and signaling. [PDF]
Peroxiredoxins (PRDXs) are a highly conserved family of peroxidases that serve as the primary scavengers of peroxides. Post-translational modifications play crucial roles modulating PRDX activities, tuning the balance between reactive oxygen species (ROS) signaling and stress. We previously reported that S-acylation occurs at the "peroxidatic" cysteine
Qiu T, Azizi SA, Pani S, Dickinson BC.
europepmc +3 more sources

