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Analysis of S-Acylation of Proteins

2003
Palmitoylation or S-acylation is the post-translational attachment of fatty acids to cysteine residues and is common among integral and peripheral mem brane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells.
Michael, Veit   +2 more
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Protein S-acylation in plants (Review)

Molecular Membrane Biology, 2009
Membrane resident proteins are a common feature of biology yet many of these proteins are not integral to the membrane. These peripheral membrane proteins are often bound to the membrane by the addition of fatty acyl chains to the protein. This modification, known as S-acylation or palmitoylation, promotes very strong membrane association but is also ...
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The emerging roles of S-acylation in autophagy

Trends in Biochemical Sciences
Autophagy is an intracellular degradation system that delivers cytoplasmic materials to the lysosome. S-acylation, a reversible post-translational modification that attaches long-chain fatty acids to cysteine residues within proteins, has recently emerged as an important regulatory mechanism for autophagy.
Jia Yao, Chunyang Xie, Aimin Yang
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Protein S-Acylation in Pulmonary Disease

Free Radical Biology and Medicine, 2016
Obesity is a major risk factor for asthma. Obese asthmatics exhibit poor symptom control, frequent exacerbation, and increased levels of reactive oxygen species (ROS). The consumption of a western diet, high in fat and carbohydrates, can both induce obesity and increase ROS.
Matthew J Randall   +4 more
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Location, location, S-acylation

Science, 2016
Plant Science![Figure][1] The stems of cellulose-deficient plants display collapsing xylem (blue). PHOTO: SIMON TURNER Cellulose synthase is a large, multisubunit machine that “swims” along the plant cell membrane as it spins out cellulose fibers. Kumar et al.
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Assaying Protein S-Acylation in Plants

2013
S-acylation is increasingly being recognized as an important posttranslational modification of proteins controlling activity, subcellular localization, microdomain residence, and stability. Heterotrimeric G-proteins and GPCRs are particularly well studied S-acylated proteins, and fast, cheap, reliable methods are required for the analysis of S ...
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Direct Analysis of Protein S-Acylation by Mass Spectrometry

2019
Dynamic and reversible protein S-acylation, most commonly occurring as S-palmitoylation, plays an important role in protein/membrane association and the regulation of intracellular signaling via cycles of palmitoylation and depalmitoylation. Direct analysis of protein S-acylation by mass spectrometry (MS) offers several benefits over indirect detection
Yuhuan, Ji, Cheng, Lin
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Protein S‐acylation, a new panacea for plant fitness

Journal of Integrative Plant Biology
ABSTRACTProtein S‐acylation or palmitoylation is a reversible post‐translational modification that influences many proteins encoded in plant genomes. Exciting progress in the past 3 years demonstrates that S‐acylation modulates subcellular localization, interacting profiles, activity, or turnover of substrate proteins in plants, participating in ...
Fei Liu, Jin‐Yu Lu, Sha Li, Yan Zhang
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Rapid and Direct Photocatalytic C(sp3)−H Acylation and Arylation in Flow

Angewandte Chemie - International Edition, 2021
Daniele Mazzarella   +2 more
exaly  

Enzymology of DHHC-mediated Protein S-Acylation

2011
Protein S-acylation is the post-translational modification of proteins with long-chain fatty acids at cysteine residues via a thioester linkage. The most commonly attached lipid is 16-carbon palmitate, thus the process is often called palmitoylation. Unlike other lipid modifications, protein S-acylation is reversible.
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