Results 21 to 30 of about 32,516 (204)
Regulation of ERK2 activity by dynamic S-acylation
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 +1 more source
Palmitoylation: a protein S-acylation with implications for breast cancer. [PDF]
NPJ Breast Cancer, 2016 AbstractProtein S-acylation is a reversible post-translational lipid modification that involves linkage of a fatty acid chain predominantly to a cysteine amino acid via a thioester bond. The fatty acid molecule is primarily palmitate, thus the term ‘palmitoylation’ is more commonly used.
Anderson AM, Ragan MA.
europepmc +7 more sources
S-acylation of P2K1 mediates extracellular ATP-induced immune signaling in Arabidopsis
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 +1 more source
Accessory proteins of the zDHHC family of S-acylation enzymes [PDF]
Journal of Cell Science, 2020 ABSTRACT Almost 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.
Christine Salaun +4 more
openaire +5 more sources
2-Bromopalmitate reduces protein deacylation by inhibition of acyl-protein thioesterase enzymatic activities. [PDF]
PLoS ONE, 2013 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
doaj +1 more source
Site-specific analysis of protein S-acylation by resin-assisted capture[S]
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
doaj +1 more source
Distinct Roles of N-Terminal Fatty Acid Acylation of the Salinity-Sensor Protein SOS3
Frontiers in Plant Science, 2021 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
Technologies and Challenges in Proteomic Analysis of Protein S-acylation [PDF]
Journal of Proteomics & Bioinformatics, 2014 Protein S-acylation (also called palmitoylation) is a pervasive post-translational modification that plays critical roles in regulating protein trafficking, localization, stability, activity, and complex formation. The past decade has witnessed tremendous advances in the study of protein S-acylation, largely owing to the development of novel S ...
Zhou, Bo +3 more
openaire +2 more sources
S‐acylation: an orchestrator of the life cycle and function of membrane proteins
The FEBS Journal, 2023 S‐acylation is a covalent post‐translational modification of proteins with fatty acids, achieved by enzymatic attachment via a labile thioester bond. This modification allows for dynamic control of protein properties and functions in association with cell membranes. This lipid modification regulates a substantial portion of the human proteome and plays
Mesquita, Francisco S. +3 more
openaire +2 more sources
Development of an Acrylamide-Based Inhibitor of Protein S-Acylation [PDF]
, 2021 Protein S-acylation is a dynamic lipid post-translational modification that can modulate the localization and activity of target proteins. In humans, the installation of the lipid onto target proteins is catalyzed by a family of 23 Asp-His-His-Cys domain-containing protein acyltransferases (DHHC-PATs).
Saara-Anne Azizi +4 more
openaire +1 more source