Evidence map›Paper›PMID 27391408›Full record

ArticleAutophagy2016

SQSTM1/p62 mediates crosstalk between autophagy and the UPS in DNA repair.

Graeme Hewitt, Bernadette Carroll, Rezazadeh Sarallah, Clara Correia-Melo, Mikołaj Ogrodnik, Glyn Nelson, Elsje G Otten, Diego Manni, Robin Antrobus, Brian A Morgan and 7 more

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

96 citing papers in PubMed, 155 citations in OpenAlex.

  1. Review
  2. ADSCs-Exo ameliorates UVB-induced skin DNA damage via p62-RNF168-dependent histone ubiquitination.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2026
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36 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

17 authors at 4 institutions in 3 countries.

Graeme Hewitta Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Bernadette Carrolla Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Rezazadeh Sarallahc Department of Biology , University of Rochester , Rochester , NY USA.
Clara Correia-Meloa Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Mikołaj Ogrodnika Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Glyn Nelsona Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Elsje G Ottena Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Diego Mannia Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Robin Antrobusb Cambridge Institute for Medical Research , Cambridge University , Cambridge , UK.
Brian A Morgana Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Thomas von Zglinickia Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Diana Jurka Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Andrei Seluanovc Department of Biology , University of Rochester , Rochester , NY USA.
Vera Gorbunovac Department of Biology , University of Rochester , Rochester , NY USA.
Terje Johansend Molecular Cancer Research Group , Department of Medical Biology , University of Tromsø - The Arctic University of Norway , Tromsø , Norway.
João F Passosa Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Viktor I Korolchuka Institute for Cell and Molecular Biosciences , Newcastle University , Newcastle upon Tyne , UK.
Newcastle University · GBUniversity of Rochester · USUiT The Arctic University of Norway · NOUniversity of Cambridge · GB

Funding

The role of hyaluronan in longevity and cancer resistance of longest-lived rodentP01AG047200 · NIA · UNIVERSITY OF ROCHESTER · PI JAN VIJG · 2014 to 2026
$36.9M
The role of SIRT6 posttranslational modifications in aging and genome stability. Supplement: Testing SIRT6 activators as potential Alzheimer's disease therapy.R01AG027237 · NIA · UNIVERSITY OF ROCHESTER · PI Vera Gorbunova · 2006 to 2026
$6.2M
Regulation of genome stability by SITR6R01AG046320 · NIA · UNIVERSITY OF ROCHESTER · PI SELUANOV, ANDREI · 2014 to 2018
$1.9M
Biotechnology and Biological Sciences Research Council BB/F010966/1Biotechnology and Biological Sciences Research Council BB/H022384/1Biotechnology and Biological Sciences Research Council BB/I020748/1NIA NIH HHS P01 AG047200NIA NIH HHS R01 AG027237NIA NIH HHS R01 AG046320
6 · The paper itself

Abstract

SQSTM1/p62 (sequestosome 1) selectively targets polyubiquitinated proteins for degradation via macroautophagy and the proteasome. Additionally, SQSTM1 shuttles between the cytoplasmic and nuclear compartments, although its role in the nucleus is relatively unknown. Here, we report that SQSTM1 dynamically associates with DNA damage foci (DDF) and regulates DNA repair. Upon induction of DNA damage SQSTM1 interacts with FLNA (filamin A), which has previously been shown to recruit DNA repair protein RAD51 (RAD51 recombinase) to double-strand breaks and facilitate homologous recombination (HR). SQSTM1 promotes proteasomal degradation of FLNA and RAD51 within the nucleus, resulting in reduced levels of nuclear RAD51 and slower DNA repair. SQSTM1 regulates the ratio between HR and nonhomologous end joining (NHEJ) by promoting the latter at the expense of the former. This SQSTM1-dependent mechanism mediates the effect of macroautophagy on DNA repair. Moreover, nuclear localization of SQSTM1 and its association with DDF increase with aging and are prevented by life-span-extending dietary restriction, suggesting that an imbalance in the mechanism identified here may contribute to aging and age-related diseases.

Indexed as

AutophagyDNA RepairAnimalsCell NucleusDNA DamageFilaminsKineticsMice, Inbred C57BLModels, BiologicalProteasome Endopeptidase ComplexProtein TransportProteolysisRad51 RecombinaseSequestosome-1 ProteinUbiquitinFilaminsProteasome Endopeptidase ComplexRad51 RecombinaseSequestosome-1 ProteinSqstm1 protein, mouseUbiquitinagingautophagyDNA damagehomologous recombinationnonhomologous end joiningSQSTM1

Identifiers

PMID27391408
PMCPMC5391493
OpenAlexW2466321927

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.