Evidence map›Paper›PMID 27601274›Full record

ArticleScientific reports2016

G-actin guides p53 nuclear transport: potential contribution of monomeric actin in altered localization of mutant p53.

Taniya Saha, Deblina Guha, Argha Manna, Abir Kumar Panda, Jyotsna Bhat, Subhrangsu Chatterjee, Gaurisankar Sa

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  5. β-Actin: An Emerging Biomarker in Ischemic Stroke.Cellular and molecular neurobiology · 2023
    Review
  6. The p53 and Calcium Regulated Actin Rearrangement in Model Cells.International journal of molecular sciences · 2022
    Article
  7. Article
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  12. Article
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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

7 authors at 1 institution in 1 country.

Taniya SahaDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata-700054, India.
Deblina GuhaDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata-700054, India.
Argha MannaDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata-700054, India.
Abir Kumar PandaDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata-700054, India.
Jyotsna BhatDivision of Biophysics, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata-700054, India.
Subhrangsu ChatterjeeDivision of Biophysics, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata-700054, India.
Gaurisankar SaDivision of Molecular Medicine, Bose Institute, P-1/12, CIT Scheme VII M, Kolkata-700054, India.
Bose Institute · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p53 preserves genomic integrity by restricting anomaly at the gene level. Till date, limited information is available for cytosol to nuclear shuttling of p53; except microtubule-based trafficking route, which utilizes minus-end directed motor dynein. The present study suggests that monomeric actin (G-actin) guides p53 traffic towards the nucleus. Histidine-tag pull-down assay using purified p53(1-393)-His and G-actin confirms direct physical association between p53 and monomeric G-actin. Co-immunoprecipitation data supports the same. Confocal imaging explores intense perinuclear colocalization between p53 and G-actin. To address atomistic details of the complex, constraint-based docked model of p53:G-actin complex was generated based on crystal structures. MD simulation reveals that p53 DNA-binding domain arrests very well the G-actin protein. Docking benchmark studies have been carried out for a known crystal structure, 1YCS (complex between p53DBD and BP2), which validates the docking protocol we adopted. Co-immunoprecipitation study using "hot-spot" p53 mutants suggested reduced G-actin association with cancer-associated p53 conformational mutants (R175H and R249S). Considering these findings, we hypothesized that point mutation in p53 structure, which diminishes p53:G-actin complexation results in mutant p53 altered subcellular localization. Our model suggests p53Arg249 form polar-contact with Arg357 of G-actin, which upon mutation, destabilizes p53:G-actin interaction and results in cytoplasmic retention of p53R249S.

Indexed as

ActinsAnimalsCell Line, TumorCell NucleusCross-Linking ReagentsDoxorubicinMolecular Dynamics SimulationMutant ProteinsPolymerizationProtein BindingProtein MultimerizationProtein TransportRabbitsSubcellular FractionsTumor Suppressor Protein p53ActinsCross-Linking ReagentsDoxorubicinMutant ProteinsTumor Suppressor Protein p53

Identifiers

PMID27601274
PMCPMC5013524
OpenAlexW2507760628

What OpenQuestion holds

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LicenceCC BY
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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.