Evidence map›Paper›PMID 20042612›Full record

ArticleThe Journal of biological chemistry2010

NAD+-dependent deacetylase SIRT3 regulates mitochondrial protein synthesis by deacetylation of the ribosomal protein MRPL10.

Yongjie Yang, Huseyin Cimen, Min-Joon Han, Tong Shi, Jian-Hong Deng, Hasan Koc, Orsolya M Palacios, Laura Montier, Yidong Bai, Qiang Tong and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
5.6field-weighted citation impact, top 5% 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

95 citing papers in PubMed, 164 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Interplay Between the Circadian Clock and Sirtuins.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Article
  10. Sirtuins in kidney health and disease.Nature reviews. Nephrology · 2024
    Review
  11. Article
  12. The role of SIRT3 in homeostasis and cellular health.Frontiers in cellular neuroscience · 2024
    Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review

35 more citing papers are in PubMed but not listed here.

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

11 authors at 3 institutions in 1 country.

Yongjie YangChildren's Nutrition Research Center, Baylor College of Medicine, Houston, Texas 77030, USA.
Huseyin Cimen
Min-Joon Han
Tong Shi
Jian-Hong Deng
Hasan Koc
Orsolya M Palacios
Laura Montier
Yidong Bai
Qiang Tong
Emine C Koc
Children's Nutrition Research Center at Baylor College of Medicine · USPennsylvania State University · USThe University of Texas Health Science Center at San Antonio · US

Funding

Role of Mitochondrial DNA Mutations in Aging in Neuronal CellsR01AG025223 · NIA · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI BAI, YIDONG · 2006 to 2010
$1.4M
Structural Studies of Mammalian Mitochondrial RibosomesR01GM071034 · NIGMS · PENNSYLVANIA STATE UNIVERSITY-UNIV PARK · PI KOC, EMINE C · 2005 to 2009
$1.3M
The Regulation of Mitochondrial Function by SIRT3R01DK075978 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI TONG, QIANG · 2006 to 2010
$1.2M
NIA NIH HHS R01 AG025223NIA NIH HHS R01AG025223NIDDK NIH HHS R01 DK075978NIDDK NIH HHS R01DK075978NIGMS NIH HHS R01 GM071034NIGMS NIH HHS R01GM071034
6 · The paper itself

Abstract

A member of the sirtuin family of NAD(+)-dependent deacetylases, SIRT3, is located in mammalian mitochondria and is important for regulation of mitochondrial metabolism, cell survival, and longevity. In this study, MRPL10 (mitochondrial ribosomal protein L10) was identified as the major acetylated protein in the mitochondrial ribosome. Ribosome-associated SIRT3 was found to be responsible for deacetylation of MRPL10 in an NAD(+)-dependent manner. We mapped the acetylated Lys residues by tandem mass spectrometry and determined the role of these residues in acetylation of MRPL10 by site-directed mutagenesis. Furthermore, we observed that the increased acetylation of MRPL10 led to an increase in translational activity of mitochondrial ribosomes in Sirt3(-/-) mice. In a similar manner, ectopic expression and knockdown of SIRT3 in C2C12 cells resulted in the suppression and enhancement of mitochondrial protein synthesis, respectively. Our findings constitute the first evidence for the regulation of mitochondrial protein synthesis by the reversible acetylation of the mitochondrial ribosome and characterize MRPL10 as a novel substrate of the NAD(+)-dependent deacetylase, SIRT3.

Indexed as

AcetylationAmino Acid SequenceAnimalsCattleCell LineHumansMiceMice, Inbred C57BLMice, KnockoutMitochondriaMitochondrial ProteinsModels, MolecularMolecular Sequence DataNADPeptidesProtein IsoformsMitochondrial ProteinsMRPL10 protein, mouseNADPeptidesProtein IsoformsRecombinant Fusion ProteinsRibosomal ProteinsSirtuin 3

Identifiers

PMID20042612
PMCPMC2844190
OpenAlexW1977199671

What OpenQuestion holds

Textmetadata
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.