Quantitative Analysis of Protein S-Acylation Site Dynamics Using Site-Specific Acyl-Biotin Exchange (ssABE).
Protein S-acylation (palmitoylation) is a reversible lipid modification that is increasingly recognized as an important regulator of protein function, including membrane association, trafficking, and subcellular localization. Most proteomic methods to study palmitoylation allow characterization of putative palmitoylated proteins but do not permit identification of individual sites of palmitoylation. We have recently adapted the Acyl-Biotin Exchange (ABE) method that is routinely used for palmitoyl-proteome characterization, to permit global S-acylation site analysis. This site-specific ABE (ssABE) protocol, when combined with SILAC-based quantification, allows both the large-scale identification of palmitoylation sites and quantitative profiling of palmitoylation site changes. This approach enables palmitoylation to be studied at a systems level comparable to other more intensively studied post-translational modifications.
['Woodley|Keith T|KT|', 'Collins|Mark O|MO|']
D000215:Acylation D001710:Biotin D002853:Chromatography, Liquid D003627:Data Interpretation, Statistical D013058:Mass Spectrometry D017293:Protein S D040901:Proteomics D013194:Staining and Labeling D053719:Tandem Mass Spectrometry D057188:Workflow
Quantitative Protein S-Acylation Palmitoylation Membrane Proteomic Mass spectrometry