Evidence map›Paper›PMID 26988914›Full record

ArticleOncotarget2016

Automethylation of SUV39H2, an oncogenic histone lysine methyltransferase, regulates its binding affinity to substrate proteins.

Lianhua Piao, Makoto Nakakido, Takehiro Suzuki, Naoshi Dohmae, Yusuke Nakamura, Ryuji Hamamoto

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Targets of histone H3 lysine 9 methyltransferases.Frontiers in cell and developmental biology · 2022
    Review
  9. Review
  10. Review
  11. Trimethyllysine: From Carnitine Biosynthesis to Epigenetics.International journal of molecular sciences · 2020
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. 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

6 authors at 3 institutions in 2 countries.

Lianhua PiaoSection of Hematology/Oncology, Department of Medicine, The University of Chicago, Chicago, IL 60637, USA.
Makoto NakakidoSection 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.
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 · JPNational Cancer Centre Japan · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously reported that the histone lysine methyltransferase SUV39H2, which is overexpressed in various types of human cancer, plays a critical role in the DNA repair after double strand breakage, and possesses oncogenic activity. Although its biological significance in tumorigenesis has been elucidated, the regulatory mechanism of SUV39H2 activity through post-translational modification is not well known. In this study, we demonstrate in vitro and in vivo automethylation of SUV39H2 at lysine 392. Automethylation of SUV39H2 led to impairment of its binding affinity to substrate proteins such as histone H3 and LSD1. Furthermore, we observed that hyper-automethylated SUV39H2 reduced methylation activities to substrates through affecting the binding affinity to substrate proteins. Our finding unveils a novel autoregulatory mechanism of SUV39H2 through lysine automethylation.

Indexed as

DNA MethylationHEK293 CellsHistone-Lysine N-MethyltransferaseHumansLysineProtein BindingProtein Processing, Post-TranslationalSubstrate SpecificityHistone-Lysine N-MethyltransferaseLysineSUV39H2 protein, humanautomethylationoncogeneSET domainSUV39H2

Identifiers

PMID26988914
PMCPMC5008405
OpenAlexW2302492885

What OpenQuestion holds

Textmetadata
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.