Evidence map›Paper›PMID 21690293›Full record

ArticleMolecular and cellular biology2011

Molecular chaperone Hsp90 regulates REV1-mediated mutagenesis.

Franklin Mayca Pozo, Tsukasa Oda, Takayuki Sekimoto, Yoshiki Murakumo, Chikahide Masutani, Fumio Hanaoka, Takayuki Yamashita

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-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

20 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
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  8. Article
  9. Mechanisms of DNA damage, repair, and mutagenesis.Environmental and molecular mutagenesis · 2017
    Review
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  11. Article
  12. Review
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  20. Stress-induced modulators of repeat instability and genome evolution.Journal of molecular microbiology and biotechnology · 2011
    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

7 authors at 4 institutions in 1 country.

Franklin Mayca PozoLaboratory of Molecular Genetics, The Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, Gunma 371-8512, Japan.
Tsukasa Oda
Takayuki Sekimoto
Yoshiki Murakumo
Chikahide Masutani
Fumio Hanaoka
Takayuki Yamashita
Gunma University · JPJapan Science and Technology Agency · JPNagoya University · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

REV1 is a Y-family polymerase that plays a central role in mutagenic translesion DNA synthesis (TLS), contributing to tumor initiation and progression. In a current model, a monoubiquitinated form of the replication accessory protein, proliferating cell nuclear antigen (PCNA), serves as a platform to recruit REV1 to damaged sites on the DNA template. Emerging evidence indicates that posttranslational mechanisms regulate REV1 in yeast; however, the regulation of REV1 in higher eukaryotes is poorly understood. Here we show that the molecular chaperone Hsp90 is a critical regulator of REV1 in human cells. Hsp90 specifically binds REV1 in vivo and in vitro. Treatment with a specific inhibitor of Hsp90 reduces REV1 protein levels in several cell types through proteasomal degradation. This is associated with suppression of UV-induced mutagenesis. Furthermore, Hsp90 inhibition disrupts the interaction between REV1 and monoubiquitinated PCNA and suppresses UV-induced focus formation. These results indicate that Hsp90 promotes folding of REV1 into a stable and/or functional form(s) to bind to monoubiquitinated PCNA. The present findings reveal a novel role of Hsp90 in the regulation of TLS-mediated mutagenesis.

Indexed as

DNA DamageMutagenesisCell LineDNA RepairHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesNuclear ProteinsNucleotidyltransferasesProliferating Cell Nuclear AntigenProtein BindingProtein FoldingUbiquitinationUltraviolet RaysY-Family DNA PolymerasesHSP90 Heat-Shock ProteinsMolecular ChaperonesNuclear ProteinsNucleotidyltransferasesProliferating Cell Nuclear AntigenREV1 protein, humanY-Family DNA Polymerases

Identifiers

PMID21690293
PMCPMC3147805
OpenAlexW2157774412

What OpenQuestion holds

Textmetadata
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.