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Updated: Jan 20, 2026

Quantification of Site-specific Protein Lysine Acetylation and Succinylation Stoichiometry Using Data-independent Acquisition Mass Spectrometry
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Mitochondria Lysine Acetylation and Phenotypic Control.

Federica Ciregia1

  • 1Department of Rheumatology, GIGA Research, Centre Hospitalier Universitaire (CHU) de Liège, University of Liège, Liège, Belgium. federica.ciregia@uliege.be.

Advances in Experimental Medicine and Biology
|August 28, 2019
PubMed
Summary

Mitochondrial lysine acetylation, a key protein modification, regulates cellular metabolism. Understanding acetylation patterns is crucial for diagnosing and treating diseases like cancer and neurodegeneration.

Keywords:
Lysine acetylationMitochondriaPost-translational modificationsProteomicsSirtuin3

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Mitochondria are central to cellular metabolism.
  • Post-translational modifications, including lysine acetylation, regulate mitochondrial protein activity.
  • Lysine acetylation involves adding an acetyl group to lysine residues, affecting protein function, interactions, and stability.

Purpose of the Study:

  • To highlight the significance of lysine acetylation in mitochondrial function.
  • To discuss the role of SIRT3 as the major mitochondrial deacetylase.
  • To explore the application of proteomics and affinity enrichment for analyzing acetylated proteins.

Main Methods:

  • Mass spectrometry-based proteomics.
  • Affinity enrichment techniques.
  • Analysis of lysine-acetylated proteins.

Main Results:

  • Lysine acetylation is an important post-translational modification in mitochondria.
  • SIRT3 is the primary mitochondrial deacetylase regulating numerous enzymes.
  • Proteomic analysis combined with affinity enrichment is the standard method for studying acetylation.

Conclusions:

  • Lysine acetylation status alterations are linked to various human diseases, including metabolic disorders, cancer, myocardial injury, and neurodegenerative diseases.
  • Further research is needed to identify specific acetylation changes with significant biological relevance.
  • Characterizing acetylation patterns in diseases is an emerging area of study.