Evidence map›Paper›PMID 26065416›Full record

ArticlePloS one2015

Proteomic Identification of DNA-PK Involvement within the RET Signaling Pathway.

Lyle J Burdine, Marie Schluterman Burdine, Linley Moreland, Brad Fogel, Lisa M Orr, Jennifer James, Richard H Turnage, Alan J Tackett

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
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 1 institution in 1 country.

Lyle J BurdineDepartment of Surgery, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
Marie Schluterman BurdineDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
Linley MorelandDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
Brad FogelDepartment of Pathology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
Lisa M OrrDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
Jennifer JamesDepartment of Pathology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
Richard H TurnageDepartment of Surgery, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
Alan J TackettDepartment of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, United States of America.
University of Arkansas for Medical Sciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Constitutive activation of the Rearranged during Transfection (RET) proto-oncogene leads to the development of MEN2A medullary thyroid cancer (MTC). The relatively clear genotype/phenotype relationship seen with RET mutations and the development of MEN2A is unusual in the fact that a single gene activity can drive the progression towards metastatic disease. Despite knowing the oncogene responsible for MEN2A, MTC, like most tumors of neural crest origin, remains largely resistant to chemotherapy. Constitutive activation of RET in a SK-N-MC cell line model reduces cell sensitivity to chemotherapy. In an attempt to identify components of the machinery responsible for the observed RET induced chemoresistance, we performed a proteomic screen of histones and associated proteins in cells with a constitutively active RET signaling pathway. The proteomic approach identified DNA-PKcs, a DNA damage response protein, as a target of the RET signaling pathway. Active DNA-PKcs, which is phosphorylated at site serine 2056 and localized to chromatin, was elevated within our model. Treatment with the RET inhibitor RPI-1 significantly reduced s2056 phosphorylation in RET cells as well as in a human medullary thyroid cancer cell line. Additionally, inhibition of DNA-PKcs activity diminished the chemoresistance observed in both cell lines. Importantly, we show that activated DNA-PKcs is elevated in medullary thyroid tumor samples and that expression correlates with expression of RET in thyroid tumors. These results highlight one mechanism by which RET signaling likely primes cells for rapid response to DNA damage and suggests DNA-PKcs as an additional target in MTC.

Indexed as

Carcinoma, NeuroendocrineCell Line, TumorDNA-Activated Protein KinaseGene Expression Regulation, NeoplasticHumansIndolesNuclear ProteinsPhosphorylationProteomicsProto-Oncogene MasProto-Oncogene Proteins c-retSignal TransductionThyroid NeoplasmsDNA-Activated Protein KinaseIndolesMAS1 protein, humanNuclear ProteinsPRKDC protein, humanProto-Oncogene MasProto-Oncogene Proteins c-retRET protein, humanRPI-1 compound

Identifiers

PMID26065416
PMCPMC4466258
OpenAlexW2256952990

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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.