Dynamics of CLIMP-63 S-acylation control ER morphology [PDF]
A key player in the formation of endoplasmic reticulum sheets is CLIMP-63, but mechanistic details remained elusive. Here authors combined cellular experiments and mathematical modelling to show that S-acylation of CLIMP-63 regulates its function by ...
Patrick A. Sandoz +12 more
doaj +4 more sources
Efficient S-Acylation of Thiourea [PDF]
Efficient S-acylation of thiourea using a variety of acid chlorides is reported. Structurally diverse aryl and alkyl substrates are compatible with this methodology.
David J. Jones +4 more
doaj +3 more sources
In vitro reconstitution of substrate S-acylation by the zDHHC family of protein acyltransferases [PDF]
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
doaj +2 more sources
Improvement of plant resistance to geminiviruses via protein de-S-acylation [PDF]
Geminiviruses are an important group of viruses that infect a variety of plants and result in heavy agricultural losses worldwide. The homologs of C4 (or L4) in monopartite geminiviruses and AC4 (or AL4) in bipartite geminiviruses are critical viral ...
Yawen Zhao +11 more
doaj +2 more sources
The landscape of renal protein S-acylation in mice with lipid-induced nephrotoxicity [PDF]
Excess 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
doaj +2 more sources
S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation [PDF]
Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular ...
Wenliang Li +12 more
doaj +2 more sources
Global, site-specific analysis of neuronal protein S-acylation [PDF]
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
doaj +6 more sources
Refining S-acylation: Structure, regulation, dynamics, and therapeutic implications. [PDF]
With a limited number of genes, cells achieve remarkable diversity. This is to a large extent achieved by chemical posttranslational modifications of proteins. Amongst these are the lipid modifications that have the unique ability to confer hydrophobicity.
Anwar MU, van der Goot FG.
europepmc +3 more sources
Fat traffic control: S-acylation in axonal transport. [PDF]
Neuronal axons serve as a conduit for the coordinated transport of essential molecular cargo between structurally and functionally distinct subcellular compartments via axonal molecular machinery. Long-distance, efficient axonal transport of membrane-bound organelles enables signal transduction and neuronal homeostasis.
Doerksen AH, Herath NN, Sanders SS.
europepmc +3 more sources
Mechanisms and functions of protein S-acylation. [PDF]
Over the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator of vital signalling pathways. S-Acylation is a reversible post-translational modification that involves the attachment of a fatty acid to a protein.
S Mesquita F +5 more
europepmc +3 more sources

