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Updated: Jul 5, 2026
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Analysis of Neutral Lipid Synthesis in Saccharomyces cerevisiae by Metabolic Labeling and Thin Layer Chromatography
Published on: February 2, 2021
Lipid Metabolic Labeling to Study Site- and Lipid-Specific Long-Chain S-Acylation Dynamics
Samiksha Sardana1,2, Carla Busquets-Hernández3, Andrea Trezza1,2
1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, Utrecht 3584 CH, The Netherlands.
ACS Chemical Biology
|July 3, 2026
Summary
Long-chain S-acylation, a key protein modification, shows diverse lipid use and site specificity. New methods reveal dynamic regulation and lipid-specific roles in cellular processes.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- Long-chain S-acylation is a crucial post-translational modification regulating cellular functions.
- The dynamic, site-, and lipid-specific patterns of protein acylation are not well understood.
Purpose of the Study:
- To investigate the site- and lipid-specific patterns of long-chain protein S-acylation.
- To explore the dynamic regulation of S-acylation and its impact on enzyme activity.
Main Methods:
- Site- and lipid-specific metabolic labeling using ω-alkynyl fatty acids.
- Investigated fatty acid incorporation into cysteines and N-terminal glycines.
- Explored the role of acyl-protein thioesterases and Palmostatin B in S-acylation dynamics.
Main Results:
- Demonstrated heterogeneity and specificity in fatty acid incorporation (C16:0, C18:0, C18:1 for S-acylation; C14:0 for N-myristoylation).
- Revealed that enzymatic specificity and metabolic context influence fatty acid incorporation.
- Uncovered dynamic S-acylation in ABHD17B, suggesting tunability of enzyme activity.
Conclusions:
- Long-chain S-acylation exhibits significant site and lipid specificity.
- Dynamic S-acylation influences protein function, exemplified by ABHD17B.
- Developed advanced lipid metabolic labeling for sensitive S-acylation studies.
