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Title: Sirtuin 2 Regulates Protein LactoylLys Modifications.

Authors: Jennings, Erin Q; Ray, Jason D; Zerio, Christopher J; Trujillo, Marissa N; McDonald, David M; Chapman, Eli; Spiegel, David A; Galligan, James J

Published In Chembiochem, (2021 Jun 15)

Abstract: Post-translational modifications (PTMs) play roles in both physiological and pathophysiological processes through the regulation of enzyme structure and function. We recently identified a novel PTM, lactoylLys, derived through a nonenzymatic mechanism from the glycolytic by-product, lactoylglutathione. Under physiologic scenarios, glyoxalase 2 prevents the accumulation of lactoylglutathione and thus lactoylLys modifications. What dictates the site-specificity and abundance of lactoylLys PTMs, however, remains unknown. Here, we report sirtuin 2 as a lactoylLys eraser. Using chemical biology and CRISPR-Cas9, we show that SIRT2 controls the abundance of this PTM both globally and on chromatin. These results address a major gap in our understanding of how nonenzymatic PTMs are regulated and controlled.

PubMed ID: 33725370 Exiting the NIEHS site

MeSH Terms: Cell Line; Humans; Models, Molecular; Molecular Structure; Protein Processing, Post-Translational; Sirtuin 2/deficiency; Sirtuin 2/metabolism*; Thiolester Hydrolases/deficiency; Thiolester Hydrolases/metabolism*

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