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    Non-enzymatic Lysine Lactoylation of Glycolytic Enzymes

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    Revised_2_Brief_Communication_ ...
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    Author
    Gaffney, Dominique O
    Jennings, Erin Q
    Anderson, Colin C
    Marentette, John O
    Shi, Taoda
    Schou Oxvig, Anne-Mette
    Streeter, Matthew D
    Johannsen, Mogens
    Spiegel, David A
    Chapman, Eli
    Roede, James R
    Galligan, James J
    Show allShow less
    Affiliation
    Univ Arizona, Dept Pharmacol & Toxicol, Coll Pharm
    Issue Date
    2020-02-20
    Keywords
    GLO2
    HAGH
    glyoxalase
    hydroxyacylglutathione hydrolase
    lactoyllysine
    lactyllysine
    methylglyoxal
    post-translational modification
    
    Metadata
    Show full item record
    Publisher
    CELL PRESS
    Citation
    Gaffney, D. O., Jennings, E. Q., Anderson, C. C., Marentette, J. O., Shi, T., Oxvig, A. M. S., ... & Roede, J. R. (2020). Non-enzymatic lysine lactoylation of glycolytic enzymes. Cell chemical biology, 27(2), 206-213. doi:10.1016/j.chembiol.2019.11.005
    Journal
    CELL CHEMICAL BIOLOGY
    Rights
    © 2019 Elsevier Ltd.
    Collection Information
    This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.
    Abstract
    Post-translational modifications (PTMs) regulate enzyme structure and function to expand the functional proteome. Many of these PTMs are derived from cellular metabolites and serve as feedback and feedforward mechanisms of regulation. We have identified a PTM that is derived from the glycolytic by-product, methylglyoxal. This reactive metabolite is rapidly conjugated to glutathione via glyoxalase 1, generating lactoylglutathione (LGSH). LGSH is hydrolyzed by glyoxalase 2 (GLO2), cycling glutathione and generating D-lactate. We have identified the non-enzymatic acyl transfer of the lactate moiety from LGSH to protein Lys residues, generating a "LactoylLys'' modification on proteins. GLO2 knockout cells have elevated LGSH and a consequent marked increase in LactoylLys. Using an alkyne-tagged methylglyoxal analog, we show that these modifications are enriched on glycolytic enzymes and regulate glycolysis. Collectively, these data suggest a previously unexplored feedback mechanism that may serve to regulate glycolytic flux under hyperglycemic or Warburg-like conditions.
    Note
    12 month embargo; published online: 22 November 2019
    ISSN
    2451-9448
    PubMed ID
    31767537
    DOI
    10.1016/j.chembiol.2019.11.005
    Version
    Final accepted manuscript
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.chembiol.2019.11.005
    Scopus Count
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    UA Faculty Publications

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