Evidence map›Paper›PMID 23453805›Full record

ArticleMolecular cell2013

ASH2L regulates ubiquitylation signaling to MLL: trans-regulation of H3 K4 methylation in higher eukaryotes.

Lipeng Wu, Shirley Y Lee, Bo Zhou, Uyen T T Nguyen, Tom W Muir, Song Tan, Yali Dou

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.9field-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

46 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  6. Review
  7. Decoding histone ubiquitylation.Frontiers in cell and developmental biology · 2022
    Review
  8. Article
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  10. Review
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  12. Article
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  14. Review
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  18. Insights on the regulation of the MLL/SET1 family histone methyltransferases.Biochimica et biophysica acta. Gene regulatory mechanisms · 2020
    Review
  19. Article
  20. 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

7 authors at 3 institutions in 1 country.

Lipeng WuDepartment of Pathology, University of Michigan, Ann Arbor, MI 48109, USA.
Shirley Y Lee
Bo Zhou
Uyen T T Nguyen
Tom W Muir
Song Tan
Yali Dou
University of Michigan–Ann Arbor · USPrinceton University · USPennsylvania State University · US

Funding

Function of MLL in transcription regulationR01GM082856 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI DOU, YALI · 2009 to 2023
$4.0M
Development and Applications of 'Designer Chromatin'R01GM107047 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2013 to 2016
$1.2M
NIGMS NIH HHS GM082856NIGMS NIH HHS R01 GM082856NIGMS NIH HHS R01 GM107047
6 · The paper itself

Abstract

Crosstalk between H2B ubiquitylation (H2Bub) and H3 K4 methylation plays important roles in coordinating functions of diverse cofactors during transcription activation. The underlying mechanism for this trans-tail signaling pathway is poorly defined in higher eukaryotes. Here, we show the following: (1) ASH2L in the MLL complex is essential for H2Bub-dependent H3 K4 methylation. Deleting or mutating K99 of the N-terminal winged helix (WH) motif in ASH2L abrogates H2Bub-dependent regulation. (2) Crosstalk can occur in trans and does not require ubiquitin to be on nucleosomes or histones to exert regulatory effects. (3) trans-regulation by ubiquitin promotes MLL activity for all three methylation states. (4) MLL3, an MLL homolog, does not respond to H2Bub, highlighting regulatory specificity for MLL family histone methyltransferases. Altogether, our results potentially expand the classic histone crosstalk to nonhistone proteins, which broadens the scope of chromatin regulation by ubiquitylation signaling.

Indexed as

UbiquitinationAmino Acid MotifsAmino Acid SubstitutionAnimalsDNA-Binding ProteinsEnzyme StabilityGene ExpressionHeLa CellsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHomeodomain ProteinsHumansMethylationModels, MolecularMutagenesis, Site-DirectedASH2L protein, humanDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistoneshomeobox protein HOXA9Homeodomain ProteinsKMT2A protein, humanMyeloid Ecotropic Viral Integration Site 1 ProteinMyeloid-Lymphoid Leukemia ProteinNeoplasm ProteinsNuclear ProteinsNucleosomesTranscription FactorsUBE2D3 protein, humanUbiquitin CUbiquitin-Conjugating EnzymesXenopus Proteins

Identifiers

PMID23453805
PMCPMC3615107
OpenAlexW1987569789

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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.