RRC ID 46238
Author Wirth M, Karaca S, Wenzel D, Ho L, Tishkoff D, Lombard DB, Verdin E, Urlaub H, Jedrusik-Bode M, Fischle W.
Title Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases.
Journal Mitochondrion
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.
Volume 13(6)
Pages 705-20
Published 2013-11-1
DOI 10.1016/j.mito.2013.02.002
PII S1567-7249(13)00026-3
PMID 23438705
PMC PMC3744624
MeSH Acetylation Animals Animals, Genetically Modified Biotin / metabolism* Caenorhabditis elegans / metabolism* Chromatography, Liquid HEK293 Cells Humans Mitochondria / enzymology Mitochondria / metabolism* Mitochondrial Proteins / metabolism* Oxidative Stress Pyruvate Carboxylase / metabolism* RNA Interference Sirtuins / metabolism* Tandem Mass Spectrometry
IF 3.992
Times Cited 8
WOS Category GENETICS & HEREDITY CELL BIOLOGY
Resource
C.elegans tm2648 tm2673