MassIVE MSV000080778

Imported Reanalysis Dataset Public PXD003530

Sites of aspirin-mediated lysine acetylation in HeLa cells

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Description

Aspirin, or acetylsalicylic acid is widely used to control pain, inflammation and fever. Important to this function is its ability to irreversibly acetylate cyclooxygenases at active site serines. Aspirin has the potential to acetylate other amino-acid side-chains, leading to speculation that aspirin-mediated lysine acetylation could explain some of its drug actions or side-effects. Using a labeled form of aspirin, aspirin-d3, we identified over 12000 sites of lysine acetylation from cultured human cells. Although aspirin amplifies acetylation signals at thousands of sites, cells tolerate aspirin mediated acetylation very well unless endogenous deacetylases are inhibited. Apart from a limited number of cellular proteins that are substantially acetylated under endogenous conditions, aspirin mediated acetylation leads to a large increase in the acetylation of many proteins even although they remain at very low stoichiometry. This reinforces the idea that a major function of cellular deacetylases is the suppression of non-specific or non-enzymatic protein acetylation. [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Aspirin ; lysine acetylation ; Hela

Contact

Principal Investigators:
(in alphabetical order) 		Ronald Thomas Hay, Centre for Gene Regulation and Expression, Sir James Black Centre, School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH. UK., N/A
Submitting User: ccms

Publications

Tatham MH, Cole C, Scullion P, Wilkie R, Westwood NJ, Stark LA, Hay RT.
A Proteomic Approach to Analyze the Aspirin-mediated Lysine Acetylome.
Mol. Cell Proteomics. 2017 Feb;16(2):310-326. Epub 2016 Dec 2.

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