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pmid:32290654
Revealing Dynamic Protein Acetylation across Subcellular Compartments.
Josue Baeza · Alexis J Lawton · Jing Fan · Michael J Smallegan · Ian Lienert · Tejas Gandhi · Oliver M Bernhardt · Lukas Reiter · John M Denu
Journal of proteome research · 2020 doi:10.1021/acs.jproteome.0c00088
Paper
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Experiment
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Data
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Analysis
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Execution
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Complete file
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Recent advances in mass spectrometry have enabled the cataloging of thousands of sites throughout the cell; however, identifying regulatory acetylation marks have proven to be a daunting task. Knowledge of the kinetics and stoichiometry of site-specific acetylation is an important factor to uncover function. Here, an improved method of quantifying acetylation stoichiometry was developed and validated, providing a detailed landscape of dynamic acetylation stoichiometry within cellular compartments. The dynamic nature of site-specific acetylation in response to serum stimulation was revealed. In two distinct human cell lines, growth factor stimulation led to site-specific, temporal acetylation changes, revealing diverse kinetic profiles that clustered into several groups. Overlap of dynamic acetylation sites among two different human cell lines suggested similar regulatory control points across major cellular pathways that include splicing, translation, and protein homeostasis. 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