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Related Experiment Video

Updated: Nov 12, 2025

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
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Sirtuin 2 Regulates Protein LactoylLys Modifications.

Erin Q Jennings1, Jason D Ray2, Christopher J Zerio1

  • 1Department of Pharmacology and Toxicology College of Pharmacy, University of Arizona, Tucson, AZ, 85721, USA.

Chembiochem : a European Journal of Chemical Biology
|March 16, 2021
PubMed
Summary
This summary is machine-generated.

Researchers discovered sirtuin 2 (SIRT2) removes lactoyllysine (lactoylLys), a novel post-translational modification. This finding explains how nonenzymatic PTMs are regulated, impacting physiological and pathophysiological processes.

Keywords:
lactoylLysmolecular modelingpost-translational modificationprotein modificationsirtuin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Post-translational modifications (PTMs) regulate protein function in physiological and pathophysiological states.
  • Lactoyllysine (lactoylLys) is a novel, nonenzymatically formed PTM from a glycolytic byproduct.
  • Glyoxalase 2 normally limits lactoylLys accumulation, but its regulation remains unclear.

Purpose of the Study:

  • To identify the enzymatic activity responsible for removing lactoylLys modifications.
  • To understand the regulation and control of nonenzymatic PTMs.
  • To investigate the role of specific enzymes in lactoylLys abundance and site-specificity.

Main Methods:

  • Chemical biology techniques to study PTMs.
  • CRISPR-Cas9 gene editing to investigate protein function.
  • Mass spectrometry-based proteomics to identify and quantify PTMs.
  • Biochemical assays to determine enzyme activity.

Main Results:

  • Sirtuin 2 (SIRT2) was identified as the primary enzyme responsible for removing lactoylLys.
  • SIRT2 activity was shown to control lactoylLys abundance globally.
  • SIRT2 was demonstrated to regulate lactoylLys modifications on chromatin.

Conclusions:

  • SIRT2 acts as a lactoylLys eraser, controlling the abundance of this nonenzymatic PTM.
  • These findings elucidate a key regulatory mechanism for nonenzymatic PTMs.
  • Understanding SIRT2's role in lactoylLys regulation has implications for various physiological and pathophysiological processes.