Evidence map›Paper›PMID 21151116›Full record

ArticleNature structural & molecular biology2011

A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability.

Pierre-Olivier Estève, Yanqi Chang, Mala Samaranayake, Anup K Upadhyay, John R Horton, George R Feehery, Xiaodong Cheng, Sriharsa Pradhan

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.

0numbers the graph read from it
0cells of the map it votes in
138citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

138 citing papers in PubMed, 223 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Lysine and arginine methylation of transcription factors.Cellular and molecular life sciences : CMLS · 2024
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

78 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Pierre-Olivier EstèveNew England Biolabs, Ipswich, Massachusetts, USA.
Yanqi Chang
Mala Samaranayake
Anup K Upadhyay
John R Horton
George R Feehery
Xiaodong Cheng
Sriharsa Pradhan
Emory University · USNew England Biolabs (United States) · US

Funding

THREE-DIMENSIONAL STRUCTURE OF HHAI METHYLASER01GM049245 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHENG, XIAODONG · 1993 to 2017
$6.6M
Histone Lysine Methylation: Structures and FunctionsR01GM068680 · NIGMS · EMORY UNIVERSITY · PI CHENG, XIAODONG · 2005 to 2012
$2.6M
NIGMS NIH HHS GM049245NIGMS NIH HHS GM068680NIGMS NIH HHS R01 GM049245NIGMS NIH HHS R01 GM068680
6 · The paper itself

Abstract

The protein lysine methyltransferase SET7 regulates DNA methyltransferase-1 (DNMT1) activity in mammalian cells by promoting degradation of DNMT1 and thus allows epigenetic changes via DNA demethylation. Here we reveal an interplay between monomethylation of DNMT1 Lys142 by SET7 and phosphorylation of DNMT1 Ser143 by AKT1 kinase. These two modifications are mutually exclusive, and structural analysis suggests that Ser143 phosphorylation interferes with Lys142 monomethylation. AKT1 kinase colocalizes and directly interacts with DNMT1 and phosphorylates Ser143. Phosphorylated DNMT1 peaks during DNA synthesis, before DNMT1 methylation. Depletion of AKT1 or overexpression of dominant-negative AKT1 increases methylated DNMT1, resulting in a decrease in DNMT1 abundance. In mammalian cells, phosphorylated DNMT1 is more stable than methylated DNMT1. These results reveal cross-talk on DNMT1, through modifications mediated by AKT1 and SET7, that affects cellular DNMT1 levels.

Indexed as

Crystallography, X-RayDNA (Cytosine-5-)-Methyltransferase 1DNA (Cytosine-5-)-MethyltransferasesDNA MethylationGenome, HumanHistone-Lysine N-MethyltransferaseHumansLysineMethylationModels, MolecularPhosphorylationProtein StabilityProtein Structure, TertiaryProto-Oncogene Proteins c-aktSerineAKT1 protein, humanDNA (Cytosine-5-)-Methyltransferase 1DNA (Cytosine-5-)-MethyltransferasesDNMT1 protein, humanHistone-Lysine N-MethyltransferaseLysineProto-Oncogene Proteins c-aktSerineSETD7 protein, human

Identifiers

PMID21151116
PMCPMC3048033
OpenAlexW2049195493

What OpenQuestion holds

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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.