Evidence map›Paper›PMID 25299772›Full record

ArticleCell death & disease2014

SMAR1 coordinates HDAC6-induced deacetylation of Ku70 and dictates cell fate upon irradiation.

N Chaudhary, K K Nakka, P L Chavali, J Bhat, S Chatterjee, S Chattopadhyay

Open access · goldAbstract read
In one paragraph

Article in Cell death & disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. CDC20: a novel therapeutic target in cancer.American journal of translational research · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. The Role of Ku70 as a Cytosolic DNA Sensor in Innate Immunity and Beyond.Frontiers in cellular and infection microbiology · 2021
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Nuclear matrix-associated protein SMAR1 regulates alternative splicing via HDAC6-mediated deacetylation of Sam68.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. Article
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 1 country.

N ChaudharyChromatin and Disease Biology Laboratory, National Centre for Cell Science, Pune University Campus, Pune, India.
K K NakkaChromatin and Disease Biology Laboratory, National Centre for Cell Science, Pune University Campus, Pune, India.
P L ChavaliChromatin and Disease Biology Laboratory, National Centre for Cell Science, Pune University Campus, Pune, India.
J BhatDepartment of Biophysics, Bose Institute, Kolkata, India.
S ChatterjeeDepartment of Biophysics, Bose Institute, Kolkata, India.
S ChattopadhyayChromatin and Disease Biology Laboratory, National Centre for Cell Science, Pune University Campus, Pune, India.
National Centre for Cell Science · INBose Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acetylation status of DNA end joining protein Ku70 dictates its function in DNA repair and Bax-mediated apoptosis. Despite the knowledge of HDACs and HATs that are reported to modulate the acetylation dynamics of Ku70, very little is known about proteins that critically coordinate these key modifications. Here, we demonstrate that nuclear matrix-associated protein scaffold/matrix-associated region-binding protein 1 (SMAR1) is a novel interacting partner of Ku70 and coordinates with HDAC6 to maintain Ku70 in a deacetylated state. Our studies revealed that knockdown of SMAR1 results in enhanced acetylation of Ku70, which leads to impaired recruitment of Ku70 in the chromatin fractions. Interestingly, ionizing radiation (IR) induces the expression of SMAR1 and its redistribution as distinct nuclear foci upon ATM-mediated phosphorylation at serine 370. Furthermore, SMAR1 regulates IR-induced G2/M cell cycle arrest by facilitating Chk2 phosphorylation. Alternatively, SMAR1 provides radioresistance by modulating the association of deacetylated Ku70 with Bax, abrogating the mitochondrial translocation of Bax. Thus, we provide mechanistic insights of SMAR1-mediated regulation of repair and apoptosis via a complex crosstalk involving Ku70, HDAC6 and Bax.

Indexed as

AcetylationAnimalsAntigens, NuclearApoptosisbcl-2-Associated X ProteinCell Cycle CheckpointsCell Cycle ProteinsCellsCheckpoint Kinase 2DNA-Binding ProteinsDNA RepairHistone Deacetylase 6Histone DeacetylasesHumansKu AutoantigenMiceAntigens, NuclearBANP protein, humanbcl-2-Associated X ProteinCell Cycle ProteinsCheckpoint Kinase 2DNA-Binding ProteinsHDAC6 protein, humanHistone Deacetylase 6Histone DeacetylasesKu AutoantigenNuclear ProteinsXrcc6 protein, humanXrcc6 protein, mouse

Identifiers

PMID25299772
PMCPMC4237237
OpenAlexW2069252486

What OpenQuestion holds

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Registered trials

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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.