Evidence map›Paper›PMID 16805913›Full record

ArticleMolecular cancer2006

Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex.

Mark A Brown, Robert J Sims, Paul D Gottlieb, Philip W Tucker

Open access · goldAbstract read
In one paragraph

Article in Molecular cancer, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers.

0numbers the graph read from it
0cells of the map it votes in
177citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

177 citing papers in PubMed, 311 citations in OpenAlex.

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  10. Epigenetics-targeted drugs: current paradigms and future challenges.Signal transduction and targeted therapy · 2024
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  17. Epigenetics.Advances in experimental medicine and biology · 2024
    Review
  18. Article
  19. Article
  20. Article

117 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

4 authors at 2 institutions in 1 country.

Mark A BrownSection of Molecular Genetics and Microbiology and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA. sambrown750@gmail.com
Robert J Sims
Paul D Gottlieb
Philip W Tucker
The University of Texas at Austin · USJohnson University · US

Funding

INTERACTION OF CIS-ACTING ELEMENTS IN CD8 REGULATIONR01AI047209 · NIAID · UNIVERSITY OF TEXAS AUSTIN · PI TUCKER, PHILIP W. · 2001 to 2005
$1.5M
Role of Bop in Cardiac Development and FunctionR01HL071160 · NHLBI · UNIVERSITY OF TEXAS AUSTIN · PI TUCKER, PHILIP W. · 2003 to 2006
$1.5M
NHLBI NIH HHS HL071160NHLBI NIH HHS R01 HL071160NIAID NIH HHS AI47209NIAID NIH HHS R01 AI047209
6 · The paper itself

Abstract

backgroundDisrupting the balance of histone lysine methylation alters the expression of genes involved in tumorigenesis including proto-oncogenes and cell cycle regulators. Methylation of lysine residues is commonly catalyzed by a family of proteins that contain the SET domain. Here, we report the identification and characterization of the SET domain-containing protein, Smyd2.

resultsSmyd2 mRNA is most highly expressed in heart and brain tissue, as demonstrated by northern analysis and in situ hybridization. Over-expressed Smyd2 localizes to the cytoplasm and the nucleus in 293T cells. Although accumulating evidence suggests that methylation of histone 3, lysine 36 (H3K36) is associated with actively transcribed genes, we show that the SET domain of Smyd2 mediates H3K36 dimethylation and that Smyd2 represses transcription from an SV40-luciferase reporter. Smyd2 associates specifically with the Sin3A histone deacetylase complex, which was recently linked to H3K36 methylation within the coding regions of active genes in yeast. Finally, we report that exogenous expression of Smyd2 suppresses cell proliferation.

conclusionWe propose that Sin3A-mediated deacetylation within the coding regions of active genes is directly linked to the histone methyltransferase activity of Smyd2. Moreover, Smyd2 appears to restrain cell proliferation, likely through direct modulation of chromatin structure.

Indexed as

Gene Expression RegulationAmino Acid SequenceAnimalsCell LineChromatinHistone-Lysine N-MethyltransferaseHistonesHumansLysineMethyltransferasesMiceMolecular Sequence DataNIH 3T3 CellsProtein Structure, TertiaryRepressor ProteinsSequence Homology, Amino AcidChromatinHistone-Lysine N-MethyltransferaseHistonesLysineMethyltransferasesRepressor ProteinsSIN3A transcription factorSin3 Histone Deacetylase and Corepressor ComplexSMYD2 protein, humanSmyd2 protein, mouse

Identifiers

PMID16805913
PMCPMC1524980
OpenAlexW2127989042

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.