Evidence map›Paper›PMID 23565200›Full record

ArticlePloS one2013

Actin polymerization negatively regulates p53 function by impairing its nuclear import in response to DNA damage.

Ling Wang, Min Wang, Shuyan Wang, Tianyang Qi, Lijing Guo, Jinjiao Li, Wenjing Qi, Khamal Kwesi Ampah, Xueqing Ba, Xianlu Zeng

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. β-Actin: An Emerging Biomarker in Ischemic Stroke.Cellular and molecular neurobiology · 2023
    Review
  6. Review
  7. Article
  8. Involvement of the Actin Machinery in Programmed Cell Death.Frontiers in cell and developmental biology · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Nuclear deformability and telomere dynamics are regulated by cell geometric constraints.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Review
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 1 institution in 1 country.

Ling WangKey Laboratory of Molecular Epigenetics of MOE and the Institute of Genetics and Cytology, Northeast Normal University, Changchun, Jilin, China.
Min Wang
Shuyan Wang
Tianyang Qi
Lijing Guo
Jinjiao Li
Wenjing Qi
Khamal Kwesi Ampah
Xueqing Ba
Xianlu Zeng
Northeast Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin, one of the most evolutionarily conservative proteins in eukaryotes, is distributed both in the cytoplasm and the nucleus, and its dynamics plays important roles in numerous cellular processes. Previous evidence has shown that actin interacts with p53 and this interaction increases in the process of p53 responding to DNA damage, but the physiological significance of their interaction remains elusive. Here, we show that DNA damage induces both actin polymerization and p53 accumulation. To further understand the implication of actin polymerization in p53 function, cells were treated with actin aggregation agent. We find that the protein level of p53 decrease. The change in p53 is a consequence of the polymeric actin anchoring p53 in the cytoplasm, thus impairing p53 nuclear import. Analysis of phosphorylation and ubiquitination of p53 reveals that actin polymerization promotes the p53 phosphorylation at Ser315 and reduces the stabilization of p53 by recruiting Aurora kinase A. Taken together, our results suggest that the actin polymerization serves as a negative modulator leading to the impairment of nuclear import and destabilization of p53. On the basis of our results, we propose that actin polymerization might be a factor participating in the process of orchestrating p53 function in response to DNA damage.

Indexed as

DNA DamageActinsActive Transport, Cell NucleusCell LineCell NucleusCytoplasmHumansOncogene Protein p21(ras)PhosphorylationProtein BindingProtein MultimerizationTumor Suppressor Protein p53UbiquitinationActinsOncogene Protein p21(ras)Tumor Suppressor Protein p53

Identifiers

PMID23565200
PMCPMC3615075
OpenAlexW1999906584

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.