Evidence map›Paper›PMID 24801886›Full record

ArticlePloS one2014

Hsc70 contributes to cancer cell survival by preventing Rab1A degradation under stress conditions.

Masako Tanaka, Saya Mun, Akihito Harada, Yasuyuki Ohkawa, Azusa Inagaki, Soichi Sano, Katsuyuki Takahashi, Yasukatsu Izumi, Mayuko Osada-Oka, Hideki Wanibuchi and 5 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 21% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

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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

15 authors at 3 institutions in 1 country.

Masako TanakaDepartment of Pharmacology, Osaka City University Medical School, Osaka, Japan.
Saya MunDepartment of Pharmacology, Osaka City University Medical School, Osaka, Japan.
Akihito HaradaDepartment of Advanced Medical Initiatives, Faculty of Medical Sciences, Kyushu University, Fukuoka, Japan.
Yasuyuki OhkawaDepartment of Advanced Medical Initiatives, Faculty of Medical Sciences, Kyushu University, Fukuoka, Japan.
Azusa InagakiDepartment of Pathology, Osaka City University Medical School, Osaka, Japan.
Soichi SanoDepartment of Cardiovascular Medicine, Osaka City University Medical School, Osaka, Japan.
Katsuyuki TakahashiDepartment of Pharmacology, Osaka City University Medical School, Osaka, Japan.
Yasukatsu IzumiDepartment of Pharmacology, Osaka City University Medical School, Osaka, Japan.
Mayuko Osada-OkaDepartment of Pharmacology, Osaka City University Medical School, Osaka, Japan.
Hideki WanibuchiDepartment of Pathology, Osaka City University Medical School, Osaka, Japan.
Masayo YamagataLaboratory of Clinical Pharmacology, Faculty of Pharmacy, Osaka Ohtani University, Tondabayashi, Japan.
Tokihito YukimuraLaboratory of Clinical Pharmacology, Faculty of Pharmacy, Osaka Ohtani University, Tondabayashi, Japan.
Katsuyuki MiuraApplied Pharmacology and Therapeutics, Osaka City University Medical School, Osaka, Japan.
Masayuki ShiotaDepartment of Pharmacology, Osaka City University Medical School, Osaka, Japan.
Hiroshi IwaoDepartment of Pharmacology, Osaka City University Medical School, Osaka, Japan.
Osaka City University · JPKyushu University · JPOsaka Ohtani University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Heat shock cognate protein 70 (Hsc70) acts as a molecular chaperone for the maintenance of intracellular proteins, which allows cancer cells to survive under proteotoxic stress. We attempted to use Hsc70 to identify key molecules in cancer cell survival. Here, we performed mass-spectrometry-based proteomics analysis utilizing affinity purification with anti-Hsc70 antibodies; as a result, 83 differentially expressed proteins were identified under stress conditions. This result implies that there was a change in the proteins with which Hsc70 interacted in response to stress. Among the proteins identified under both serum-depleted and 5-fluorouracil-treated conditions, Rab1A was identified as an essential molecule for cancer cell survival. Hsc70 interacted with Rab1A in a chaperone-dependent manner. In addition, Hsc70 knockdown decreased the level of Rab1A and increased the level of its ubiquitination under stress conditions, suggesting that Hsc70 prevented the degradation of Rab1A denatured by stress exposure. We also found that Rab1A knockdown induced cell death by inhibition of autophagosome formation. Rab1A may therefore contribute to overcoming proteotoxic insults, which allows cancer cells to survive under stress conditions. Analysis of Hsc70 interactors provided insight into changes of intracellular status. We expect further study of the Hsc70 interactome to provide a more comprehensive understanding of cancer cell physiology.

Indexed as

ApoptosisAutophagyCell SurvivalFluorouracilGene Expression RegulationHSC70 Heat-Shock ProteinsHT29 CellsHumansProtein Array AnalysisProteinsProteomicsrab1 GTP-Binding ProteinsRNA InterferenceRNA, Small InterferingFluorouracilHSC70 Heat-Shock ProteinsProteinsrab1 GTP-Binding ProteinsRNA, Small Interfering

Identifiers

PMID24801886
PMCPMC4011886
OpenAlexW1982875845

What OpenQuestion holds

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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.