Evidence map›Paper›PMID 26219988›Full record

ArticleScientific reports2015

Sirt1-deficiency causes defective protein quality control.

Takuya Tomita, Jun Hamazaki, Shoshiro Hirayama, Michael W McBurney, Hideki Yashiroda, Shigeo Murata

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

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  5. NADInternational journal of molecular sciences · 2024
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  16. Could Sirtuin Activities Modify ALS Onset and Progression?Cellular and molecular neurobiology · 2017
    Review
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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

6 authors at 2 institutions in 2 countries.

Takuya TomitaLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Jun HamazakiLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Shoshiro HirayamaLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Michael W McBurneyCenter for Cancer Therapeutics, Ottawa Hospital Research Institute, Ottawa, Ontario, Canada.
Hideki YashirodaLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Shigeo MurataLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
The University of Tokyo · JPOttawa Hospital Research Institute

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein quality control is an important mechanism to maintain cellular homeostasis. Damaged proteins have to be restored or eliminated by degradation, which is mainly achieved by molecular chaperones and the ubiquitin-proteasome system. The NAD(+)-dependent deacetylase Sirt1 has been reported to play positive roles in the regulation of cellular homeostasis in response to various stresses. However, its contribution to protein quality control remains unexplored. Here we show that Sirt1 is involved in protein quality control in both an Hsp70-dependent and an Hsp70-independent manner. Loss of Sirt1 led to the accumulation of ubiquitinated proteins in cells and tissues, especially upon heat stress, without affecting proteasome activities. This was partly due to decreased basal expression of Hsp70. However, this accumulation was only partially alleviated by overexpression of Hsp70 or induction of Hsp70 upon heat shock in Sirt1-deficient cells and tissues. These results suggest that Sirt1 mediates both Hsp70-dependent and Hsp70-independent protein quality control. Our findings cast new light on understanding the role of Sirt1 in maintaining cellular homeostasis.

Indexed as

AnimalsCell LineDNA-Binding ProteinsHeat-Shock ResponseHomeostasisHSP70 Heat-Shock ProteinsMiceMolecular ChaperonesProteasome Endopeptidase ComplexSirtuin 1UbiquitinUbiquitin-Protein LigasesDNA-Binding ProteinsHSP70 Heat-Shock ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexSirt1 protein, mouseSirtuin 1UbiquitinUbiquitin-Protein Ligases

Identifiers

PMID26219988
PMCPMC4518232
OpenAlexW2414611358

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LicenceCC BY
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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.