Evidence map›Paper›PMID 19089598›Full record

ArticleCell stress & chaperones2009

Hsp70 translocates to the nuclei and nucleoli, binds to XRCC1 and PARP-1, and protects HeLa cells from single-strand DNA breaks.

Polychronis Kotoglou, Alexandros Kalaitzakis, Patra Vezyraki, Theodore Tzavaras, Lampros K Michalis, Francoise Dantzer, Jae U Jung, Charalampos Angelidis

Open access · greenAbstract read
In one paragraph

Article in Cell stress & chaperones, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

53 citing papers in PubMed, 98 citations in OpenAlex.

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  18. The Nuclear and DNA-Associated Molecular Chaperone Network.Cold Spring Harbor perspectives in biology · 2019
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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

8 authors at 3 institutions in 3 countries.

Polychronis KotoglouLaboratory of General Biology, Medical School, University of Ioannina, Ioannina, Greece.
Alexandros Kalaitzakis
Patra Vezyraki
Theodore Tzavaras
Lampros K Michalis
Francoise Dantzer
Jae U Jung
Charalampos Angelidis
University of Ioannina · GRÉcole Supérieure de Biotechnologie de Strasbourg · FRHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For many years, there has been uncertainty concerning the reason for Hsp70 translocation to the nucleus and nucleolus. Herein, we propose that Hsp70 translocates to the nucleus and nucleoli in order to participate in pathways related to the protection of the nucleoplasmic DNA or ribosomal DNA from single-strand breaks. The absence of Hsp70 in HeLa cells, via Hsp70 gene silencing (knockdown), indicated the essential role of Hsp70 in DNA integrity. Therefore, HeLa Hsp70 depleted cells were very sensitive in heat treatment and their DNA breaks were multiple compared to that of control HeLa cells. The molecular mechanism with which Hsp70 performs its role at the level of nucleus and nucleolus during stress was examined. Hsp70 co-localizes with PARP1 in the nucleus/nucleoli as was observed in confocal studies and binds to the BCRT domain of PARP1 as was revealed with protein-protein interaction assays. It was also found that Hsp70 binds simultaneously to XRCC1 and PARP-1, indicating that Hsp70 function takes place at the level of DNA repair and possibly at the base excision repair system. Making a hypothetical model, we have suggested that Hsp70 is the molecule that binds and interrelates with PARP1 creating the repair proteins simultaneously, such as XRCC1, at the single-strand DNA breaks. Our data partially clarify a previously unrecognized cellular response to heat stress. Finally, we can speculate that Hsp70 plays a role in the quality and integrity of DNA.

Indexed as

DNA Breaks, Single-StrandedActive Transport, Cell NucleusApoptosisCell Line, TumorCell NucleolusCell NucleusDNA-Binding ProteinsDNA, Single-StrandedHeLa CellsHot TemperatureHSP70 Heat-Shock ProteinsHumansPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProtein Structure, TertiaryRNA, Small InterferingDNA-Binding ProteinsDNA, Single-StrandedHSP70 Heat-Shock ProteinsPARP1 protein, humanPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesRNA, Small InterferingX-ray Repair Cross Complementing Protein 1XRCC1 protein, human

Identifiers

PMID19089598
PMCPMC2728274
OpenAlexW1967439927

What OpenQuestion holds

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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.