出版社：American Society for Biochemistry and Molecular Biology
摘要：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.
