Proteomic analysis of fatty-acylated proteins

• Protein fatty-acylation regulates many fundamental biological processes in eukaryotes.
• Chemical proteomics has expanded the potential functions of protein fatty-acylation in biology.
• New methods are needed for direct identification of fatty-acylation sites and characterization of covalently attached lipids.
• Quantitative methods are desired for functional characterization of fatty-acylation regulatory mechanisms.

Protein fatty-acylation in eukaryotes has been associated with many fundamental biological processes. However, the diversity, abundance and regulatory mechanisms of protein fatty-acylation in vivo remain to be explored. Herein, we review the proteomic analysis of fatty-acylated proteins, with a focus on N-myristoylation and S-palmitoylation. We then highlight major challenges and emerging methods for direct site identification, quantitation, and lipid structure characterization to understand the functions and regulatory mechanisms of fatty-acylated proteins in physiology and disease.

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