Evidence map›Paper›PMID 24962791›Full record

ArticleMolecular oncology2014

TRAP1-dependent regulation of p70S6K is involved in the attenuation of protein synthesis and cell migration: relevance in human colorectal tumors.

Danilo Swann Matassa, Ilenia Agliarulo, Maria Rosaria Amoroso, Francesca Maddalena, Leandra Sepe, Maria Carla Ferrari, Vinay Sagar, Silvia D'Amico, Fabrizio Loreni, Giovanni Paolella and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular oncology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

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  20. Overexpression of tumor necrosis factor receptor-associated protein 1 (TRAP1) are associated with poor prognosis of epithelial ovarian cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
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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

12 authors at 5 institutions in 1 country.

Danilo Swann MatassaDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Ilenia AgliaruloDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Maria Rosaria AmorosoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy.
Francesca MaddalenaLaboratory of Pre-Clinical and Translational Research, IRCCS, Referral Cancer Center of Basilicata, Rionero in Vulture, PZ, Italy.
Leandra SepeDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy; Ceinge Biotecnologie Avanzate, Via G. Salvatore 486, 80145 Naples, Italy.
Maria Carla FerrariDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy; Ceinge Biotecnologie Avanzate, Via G. Salvatore 486, 80145 Naples, Italy.
Vinay SagarDepartment of Biology, University of Rome 'Tor Vergata', Via Ricerca Scientifica, Rome 00133, Italy.
Silvia D'AmicoDepartment of Biology, University of Rome 'Tor Vergata', Via Ricerca Scientifica, Rome 00133, Italy.
Fabrizio LoreniDepartment of Biology, University of Rome 'Tor Vergata', Via Ricerca Scientifica, Rome 00133, Italy.
Giovanni PaolellaDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy; Ceinge Biotecnologie Avanzate, Via G. Salvatore 486, 80145 Naples, Italy.
Matteo LandriscinaClinical Oncology Unit, Department of Medical and Surgical Sciences, University of Foggia, Foggia, Italy.
Franca EspositoDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Naples, Italy. Electronic address: franca.esposito@unina.it.
University of Naples Federico II · ITCeinge Biotecnologie Avanzate (Italy) · ITUniversity of Rome Tor Vergata · ITCentro di Riferimento Oncologico della Basilicata · ITUniversity of Foggia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TNF receptor-associated protein 1 (TRAP1) is an HSP90 chaperone involved in stress protection and apoptosis in mitochondrial and extramitochondrial compartments. Remarkably, aberrant deregulation of TRAP1 function has been observed in several cancer types with potential new opportunities for therapeutic intervention in humans. Although previous studies by our group identified novel roles of TRAP1 in quality control of mitochondria-destined proteins through the attenuation of protein synthesis, molecular mechanisms are still largely unknown. To shed further light on the signaling pathways regulated by TRAP1 in the attenuation of protein synthesis, this study demonstrates that the entire pathway of cap-mediated translation is activated in cells following TRAP1 interference: consistently, expression and consequent phosphorylation of p70S6K and RSK1, two translation activating kinases, are increased upon TRAP1 silencing. Furthermore, we show that these regulatory functions affect the response to translational stress and cell migration in wound healing assays, processes involving both kinases. Notably, the regulatory mechanisms controlled by TRAP1 are conserved in colorectal cancer tissues, since an inverse correlation between TRAP1 and p70S6K expression is found in tumor tissues, thereby supporting the relevant role of TRAP1 translational regulation in vivo. Taken as a whole, these new findings candidate TRAP1 network for new anti-cancer strategies aimed at targeting the translational/quality control machinery of tumor cells.

Indexed as

Cell MovementColorectal NeoplasmsHCT116 CellsHSP90 Heat-Shock ProteinsHumansImmunoprecipitationMicroscopy, ConfocalProtein BiosynthesisRibosomal Protein S6 Kinases, 70-kDaHSP90 Heat-Shock ProteinsRibosomal Protein S6 Kinases, 70-kDaTRAP1 protein, humanCell migrationColorectal carcinomaRibavirinTranslation controlTRAP1Wound healing

Identifiers

PMID24962791
PMCPMC5528605
OpenAlexW2015263527

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.