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ARF1-Flag and its palmitoylation-deficient mutant (C159A-Flag) were purified by immunoprecipitation separately. The purified proteins were digested and analyzed by LC-MS-based quantitative proteomics to identify differential interactors and binding affinity changes induced by ARF1 palmitoylation. This study is essential for understanding how palmitoylation regulates ARF1 function and its underlying mechanisms.