Mass-tag labeling reveals site-specific and endogenous levels of protein S-fatty acylation

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Abstract
Significance: Cysteine fatty acylation (S-fatty acylation) regulates the stability, trafficking, and activity of proteins in eukaryotes. Current methods to study S-fatty acylation rely on the metabolic incorporation of fatty acid analogs or selective chemical labeling and affinity purification, which limits the detection of endogenous S-fatty acylated protein isoforms and levels. Here we demonstrate that the biochemical exchange of acyl groups on cysteines with defined mass-tags enables the direct visualization of endogenous S-fatty acylated protein levels. The application of this mass-tag labeling method revealed that site-specific S-fatty acylation of interferon-induced transmembrane protein 3 controls the antiviral activity of this IFN-induced effector.
Funding Information
  • HHS | NIH | National Institute of General Medical Sciences (R01GM087544)
  • Starr Cancer Consortium (I7-A717)
  • HHS | NIH | National Institute of Allergy and Infectious Diseases (R56AI114826)
  • HHS | NIH | National Institute of Allergy and Infectious Diseases (R00AI095348)

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