Evidence map›Paper›PMID 23438705›Full record

ArticleMitochondrion2013

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

Open access · greenAbstract read
In one paragraph

Article in Mitochondrion, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.7field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 23 citations in OpenAlex.

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  15. For Certain, SIRT4 Activities!Trends in biochemical sciences · 2017
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 5 institutions in 2 countries.

Martina WirthLaboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Samir Karaca
Dirk Wenzel
Linh Ho
Daniel Tishkoff
David B Lombard
Eric Verdin
Henning Urlaub
Monika Jedrusik-Bode
Wolfgang Fischle
Max Planck Institute for Biophysical Chemistry · DEMax Planck Society · DEUniversity of Michigan–Ann Arbor · USGladstone Institutes · USUniversity of California, San Francisco · US

Funding

Virology CoreP30AI027763 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STEVEN Grant DEEKS · 1988 to 2026
$93.6M
Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
REVERSIBLE MITOCHONDRIAL PROTEIN ACETYLATION AND METABOLIC REGULATIONR24DK085610 · NIDDK · J. DAVID GLADSTONE INSTITUTES · PI VERDIN, ERIC M. · 2010 to 2019
$16.0M
Research Training in BiogerontologyT32AG000114 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCOTT PLETCHER · 1985 to 2026
$12.4M
RESEARCH TRAINING IN CHEMISTRY AND CHEMICAL BIOLOGYT32GM064337 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2002 to 2021
$7.8M
Regulation of one carbon metabolism and epigenetics by SIRT5R01GM101171 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LOMBARD, DAVID BENNER · 2012 to 2021
$2.6M
A Technological Platform for the Identification of Serine Proteases in CancerR01CA128765 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CRAIK, CHARLES SCOTT · 2009 to 2011
$1.1M
NCI NIH HHS R01 CA128765NIAID NIH HHS P30 AI027763NIA NIH HHS T32 AG000114NIA NIH HHS T32-AG000114, DTNIDDK NIH HHS DK085610NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R24 DK085610NIGMS NIH HHS 1R01GM101171NIGMS NIH HHS R01 GM101171NIGMS NIH HHS T32 GM064337
6 · The paper itself

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.

Indexed as

AcetylationAnimalsAnimals, Genetically ModifiedBiotinCaenorhabditis elegansChromatography, LiquidHEK293 CellsHumansMitochondriaMitochondrial ProteinsOxidative StressPyruvate CarboxylaseRNA InterferenceSirtuinsTandem Mass SpectrometryBiotinMitochondrial ProteinsPyruvate CarboxylaseSirtuinsBiotin-dependent carboxylaseC. elegansProtein acetylationPyruvate carboxylaseSIRT4Sirtuins

Identifiers

PMID23438705
PMCPMC3744624
OpenAlexW2047413506

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.