Evidence map›Paper›PMID 26586479›Full record

ArticleOncotarget2015

SUV420H1 enhances the phosphorylation and transcription of ERK1 in cancer cells.

Theodore Vougiouklakis, Kenbun Sone, Vassiliki Saloura, Hyun-Soo Cho, Takehiro Suzuki, Naoshi Dohmae, Houda Alachkar, Yusuke Nakamura, Ryuji Hamamoto

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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  5. Article
  6. The SUV4-20H Histone Methyltransferases in Health and Disease.International journal of molecular sciences · 2022
    Review
  7. Differential effects by sex with Kmt5b loss.Autism research : official journal of the International Society for Autism Research · 2021
    Article
  8. Observational
  9. Review
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  14. Review
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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 2 institutions in 2 countries.

Theodore VougiouklakisSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Kenbun SoneSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Vassiliki SalouraSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Hyun-Soo ChoSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Takehiro SuzukiBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Houda AlachkarSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Yusuke NakamuraSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Ryuji HamamotoSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
University of Chicago · USRIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The oncogenic protein ERK, a member of the extracellular signal-regulated kinase (ERK) cascade, is a well characterized signaling molecule involved in tumorigenesis. The ERK signaling pathway is activated in a large proportion of cancers and plays a critical role in tumor development. Functional regulation by phosphorylation of kinases in the ERK pathway has been extensively studied, however methylation of the ERK protein has not been reported to date. Here, we demonstrated that the protein lysine methyltransferase SUV420H1 tri-methylated ERK1 at lysines 302 and 361, and that substitution of methylation sites diminished phosphorylation levels of ERK1. Concordantly, knockdown of SUV420H1 reduced phosphorylated ERK1 and total ERK1 proteins, and interestingly suppressed ERK1 at the transcriptional level. Our results indicate that overexpression of SUV420H1 may result in activation of the ERK signaling pathway through enhancement of ERK phosphorylation and transcription, thereby providing new insights in the regulation of the ERK cascade in human cancer.

Indexed as

Transcription, GeneticBlotting, WesternCarcinogenesisCell Line, TumorCell ProliferationGene Expression Regulation, NeoplasticHistone-Lysine N-MethyltransferaseHumansMAP Kinase Signaling SystemMass SpectrometryMitogen-Activated Protein Kinase 3NeoplasmsPhosphorylationReal-Time Polymerase Chain ReactionRNA, Small InterferingTransfectionHistone-Lysine N-MethyltransferaseKMT5C protein, humanMitogen-Activated Protein Kinase 3RNA, Small InterferingERK1non-histone protein methylationprotein lysine methyltransferaseSUV420H1

Identifiers

PMID26586479
PMCPMC4791223
OpenAlexW2276282242

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.