| RRC ID |
46238
|
| 著者 |
Wirth M, Karaca S, Wenzel D, Ho L, Tishkoff D, Lombard DB, Verdin E, Urlaub H, Jedrusik-Bode M, Fischle W.
|
| タイトル |
Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals interact with pyruvate carboxylase and other acetylated biotin-dependent carboxylases.
|
| ジャーナル |
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.
|
| 巻・号 |
13(6)
|
| ページ |
705-20
|
| 公開日 |
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
|
| 引用数 |
8
|
|
WOS 分野
|
GENETICS & HEREDITY
CELL BIOLOGY
|
| リソース情報 |
| 線虫 |
tm2648
tm2673 |
