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Related Experiment Video

Updated: May 30, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates

Published on: February 27, 2016

Murine Sirt3 protein isoforms have variable half-lives.

Yongjie Yang1, Ke Yun Chen, Qiang Tong

  • 1Children's Nutrition Research Center, Baylor College of Medicine, 1100 Bates Street, Houston, TX 77030, USA.

Gene
|August 16, 2011
PubMed
Summary

The Sirt3 protein has three isoforms (M1, M2, M3). M1 and M2 are stable in mitochondria, but M3 is rapidly degraded by proteasomes, potentially involving Skp2 and HSP60 interactions.

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Area of Science:

  • Mitochondrial biology
  • Protein biochemistry
  • Molecular genetics

Background:

  • Sirtuin 3 (Sirt3) is a mitochondrial NAD+-dependent deacetylase.
  • Murine Sirt3 gene variants produce three protein isoforms: M1, M2, and M3.
  • Differential stability and function of Sirt3 isoforms are not fully understood.

Purpose of the Study:

  • To investigate the expression stability and degradation mechanisms of Sirt3 protein isoforms (M1, M2, M3).
  • To identify factors contributing to the instability of the Sirt3 M3 isoform.
  • To explore potential roles of protein interactions in Sirt3 isoform stability.

Main Methods:

  • Stable expression of Sirt3 M1, M2, and M3 variants in cell lines.
  • Treatment with proteasome inhibitors to assess degradation pathways.

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Last Updated: May 30, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
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Published on: February 27, 2016

Measurement of Protein Turnover Rates in Senescent and Non-Dividing Cultured Cells with Metabolic Labeling and Mass Spectrometry
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Measurement of Protein Turnover Rates in Senescent and Non-Dividing Cultured Cells with Metabolic Labeling and Mass Spectrometry

Published on: April 6, 2022

  • Ubiquitination assays and identification of E3 ubiquitin ligase subunits.
  • Co-immunoprecipitation to study protein-protein interactions, including with HSP60.

    • Main Results:

    • Sirt3 M1 and M2 isoforms exhibit stable mitochondrial expression.
    • Sirt3 M3 isoform shows very low expression due to rapid proteasomal degradation.
    • Proteasome inhibition and Skp2 involvement were confirmed in Sirt3 M3 degradation.
    • Sirt3 M1 and M2, but not M3, specifically interact with heat shock protein 60 (HSP60).

    Conclusions:

    • The Sirt3 M3 isoform is inherently unstable and targeted for rapid proteasomal degradation.
    • The E3 ubiquitin ligase subunit Skp2 is implicated in Sirt3 M3 degradation.
    • Interaction with HSP60 may contribute to the stability of Sirt3 M1 and M2 isoforms, suggesting a role for heat shock proteins in regulating Sirt3 protein stability.