Evidence map›Paper›PMID 24586549›Full record

ArticlePloS one2014

Rac1 participates in thermally induced alterations of the cytoskeleton, cell morphology and lipid rafts, and regulates the expression of heat shock proteins in B16F10 melanoma cells.

Burcin Gungor, Imre Gombos, Tim Crul, Ferhan Ayaydin, László Szabó, Zsolt Török, Lajos Mátés, László Vígh, Ibolya Horváth

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.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.4field-weighted citation impact, top 19% 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, 30 citations in OpenAlex.

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  15. BGP-15 improves contractile function of regenerating soleus muscle.Journal of muscle research and cell motility · 2018
    Article
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  19. BGP-15 prevents the death of neurons in a mouse model of familial dysautonomia.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

9 authors at 4 institutions in 1 country.

Burcin GungorInstitute of Biochemistry, Laboratory of Molecular Stress Biology, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
Imre GombosInstitute of Biochemistry, Laboratory of Molecular Stress Biology, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
Tim CrulInstitute of Biochemistry, Laboratory of Molecular Stress Biology, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
Ferhan AyaydinLaboratory of Cellular Imaging, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
László SzabóInstitute of Material and Environmental Chemistry, Department of Functional and Structural Materials, Research Center for Natural Sciences, Budapest, Hungary.
Zsolt TörökInstitute of Biochemistry, Laboratory of Molecular Stress Biology, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
Lajos MátésInstitute of Genetics, Laboratory of Cancer Genome Research, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
László VíghInstitute of Biochemistry, Laboratory of Molecular Stress Biology, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
Ibolya HorváthInstitute of Biochemistry, Laboratory of Molecular Stress Biology, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary.
Hungarian Academy of Sciences · HUHUN-REN Szegedi Biológiai Kutatóközpont · HUInstitute of Genetics · HUInstitute of Materials and Environmental Chemistry · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic cells exhibit a characteristic response to hyperthermic treatment, involving morphological and cytoskeletal alterations and the induction of heat shock protein synthesis. Small GTPases of the Ras superfamily are known to serve as molecular switches which mediate responses to extracellular stimuli. We addressed here how small GTPase Rac1 integrates signals from heat stress and simultaneously induces various cellular changes in mammalian cells. As evidence that Rac1 is implicated in the heat shock response, we first demonstrated that both mild (41.5°C) and severe (43°C) heat shock induced membrane translocation of Rac1. Following inhibition of the activation or palmitoylation of Rac1, the size of its plasma membrane-bound pool was significantly decreased while the heat shock-induced alterations in the cytoskeleton and cell morphology were prevented. We earlier documented that the size distribution pattern of cholesterol-rich rafts is temperature dependent and hypothesized that this is coupled to the triggering mechanism of stress sensing and signaling. Interestingly, when plasma membrane localization of Rac1 was inhibited, a different and temperature independent average domain size was detected. In addition, inhibition of the activation or palmitoylation of Rac1 resulted in a strongly decreased expression of the genes of major heat shock proteins hsp25 and hsp70 under both mild and severe heat stress conditions.

Indexed as

Heat-Shock ResponseActin CytoskeletonAnimalsCholesterolCytoskeletonGene Expression Regulation, NeoplasticHeat-Shock ProteinsHSP70 Heat-Shock ProteinsLipoylationMelanoma, ExperimentalMembrane FluidityMembrane MicrodomainsMiceMolecular ChaperonesNeoplasm ProteinsProtein TransportCholesterolHeat-Shock ProteinsHsbp1 protein, mouseHSP70 Heat-Shock ProteinsMolecular ChaperonesNeoplasm Proteinsrac1 GTP-Binding Protein

Identifiers

PMID24586549
PMCPMC3930703
OpenAlexW2054822441

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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.