J Lipid Res
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Published: February 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. Although this modification is a well-recognized determinant of protein function and localization, current techniques to study cellular S-acylation are cumbersome and/or technically demanding. We recently described a simple and robust methodology to rapidly identify S-nitrosylation sites in proteins via resin-assisted capture (RAC) and provided an initial description of the applicability of the technique to S-acylated proteins (acyl-RAC). Here we expand on the acyl-RAC assay, coupled with mass spectrometry-based proteomics, to characterize both previously reported and novel sites of endogenous S-acylation. Acyl-RAC should therefore find general applicability in studies of both global and individual protein S-acylation in mammalian cells.
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http://dx.doi.org/10.1194/jlr.D011106 | DOI Listing |
The Golgi apparatus is a critical organelle responsible for intracellular trafficking and signaling, orchestrating essential processes such as protein and lipid sorting . Dysregulation of its function has been implicated in various pathologies, including obesity, diabetes, and cancer, highlighting its importance as a potential therapeutic target. Despite this, the development of tools to selectively target the Golgi in specific cell types remain a significant unmet challenge in imaging and drug discovery.
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Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe, 657-8501, Japan. Electronic address:
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School of Pharmacy and BioMolecular Sciences, Liverpool John Moores University, Byram Street, Liverpool L3 3AF, UK.
Protein S-acyl transferases (PATs) are a family of enzymes that catalyze protein S-acylation, a post-translational lipid modification involved in protein membrane targeting, trafficking, stability, and protein-protein interaction. S-acylation plays important roles in plant growth, development, and stress responses. Here, we report the genome-wide analysis of the family genes in the woodland strawberry (), a model plant for studying the economically important Rosaceae family.
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Department of Pathology, Faculty of Medicine, Dalhousie University, Halifax, NS, Canada.
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