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Comment
. 2017 Feb 16;24(2):126-128.
doi: 10.1016/j.chembiol.2017.01.011.

A Prob(e)able Route to Lysine Acylation

Gregory R Wagner  1 , Matthew D Hirschey  2
Affiliations
Comment

A Prob(e)able Route to Lysine Acylation

Gregory R Wagner et al. Cell Chem Biol. .

Abstract

Non-enzymatic modification of proteins by acyl-CoA species involved in intermediary metabolism is a possible explanation for widespread protein acylation. In this issue, Kulkarni et al. (2017) develop a set of chemoproteomic probes to interrogate the role of malonyl-CoA in mediating protein malonylation and find malonylation influences glycolysis in cancer cells.

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Comment on

  • Discovering Targets of Non-enzymatic Acylation by Thioester Reactivity Profiling.
    Kulkarni RA, Worth AJ, Zengeya TT, Shrimp JH, Garlick JM, Roberts AM, Montgomery DC, Sourbier C, Gibbs BK, Mesaros C, Tsai YC, Das S, Chan KC, Zhou M, Andresson T, Weissman AM, Linehan WM, Blair IA, Snyder NW, Meier JL. Kulkarni RA, et al. Cell Chem Biol. 2017 Feb 16;24(2):231-242. doi: 10.1016/j.chembiol.2017.01.002. Epub 2017 Feb 2. Cell Chem Biol. 2017. PMID: 28163016 Free PMC article.

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