Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases

Martina Wirth, Samir Karaca, Dirk Wenzel, Linh Ho, Daniel Tishkoff, David B. Lombard, Eric Verdin, Henning Urlaub, Monika Jedrusik-Bode*, Wolfgang Fischle

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

The biological and enzymatic function of SIRT4 is largely uncharacterized. We show that the Caenorhabditis elegans SIR-2.2 and SIR-2.3 orthologs of SIRT4 are ubiquitously expressed, also localize to mitochondria and function during oxidative stress. Further, we identified conserved interaction with mitochondrial biotin-dependent carboxylases (PC, PCC, MCCC), key enzymes in anaplerosis and ketone body formation. The carboxylases were found acetylated on multiple lysine residues and detailed analysis of mPC suggested that one of these residues, K748ac, might regulate enzymatic activity. Nevertheless, no changes in mPC acetylation levels and enzymatic activity could be detected upon overexpression or loss of functional SIRT4.

Original languageEnglish (US)
Pages (from-to)705-720
Number of pages16
JournalMitochondrion
Volume13
Issue number6
DOIs
StatePublished - Nov 1 2013

Keywords

  • Biotin-dependent carboxylase
  • C. elegans
  • Protein acetylation
  • Pyruvate carboxylase
  • SIRT4
  • Sirtuins

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology
  • Cell Biology

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