Evidence map›Paper›PMID 20523115›Full record

ReviewEpigenetics2010

Histone H2B ubiquitination and beyond: Regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation.

Mahesh B Chandrasekharan, Fu Huang, Zu-Wen Sun

Open access · bronzeAbstract readReview
In one paragraph

Review in Epigenetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

81 citing papers in PubMed, 118 citations in OpenAlex.

  1. Review
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  11. Article
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  14. Review
  15. Histone modification inComputational and structural biotechnology journal · 2023
    Review
  16. Multistate structures of the MLL1-WRAD complex bound to H2B-ubiquitinated nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Review
  18. Decoding histone ubiquitylation.Frontiers in cell and developmental biology · 2022
    Review
  19. Epigenetic Regulation of Nucleotide Excision Repair.Frontiers in cell and developmental biology · 2022
    Review
  20. Article

21 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

3 authors at 1 institution in 1 country.

Mahesh B ChandrasekharanDepartment of Biochemistry and Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville, TN, USA.
Fu Huang
Zu-Wen Sun
Vanderbilt University · US

Funding

TISSUE CoreP50CA098131 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI PARK, BEN HO, PIETENPOL, JENNIFER A · 2003 to 2024
$48.7M
Functions of Histone Ubiquitination and MethylationR01CA109355 · NCI · VANDERBILT UNIVERSITY · PI SUN, ZU-WEN · 2006 to 2010
$1.2M
NCI NIH HHS 5P0CA098131NCI NIH HHS P50 CA098131NCI NIH HHS R01 CA109355NCI NIH HHS R01CA109355
6 · The paper itself

Abstract

Regulation of Set1-COMPASS-mediated H3K4 methylation and Dot1-mediated H3K79 methylation by H2BK123 ubiquitination (H2Bub1) is an evolutionarily conserved trans-histone crosstalk mechanism. How H2Bub1 impacts chromatin structure and affects Set1-COMPASS/Dot1 functions has not been fully defined. Ubiquitin was proposed to bind proteins to physically bridge H2Bub1 with Set1-COMPASS/Dot1. Alternatively, the bulky ubiquitin was thought to be a "wedge" that loosens the nucleosome for factor access. Contrary to the latter possibility, recent discoveries provide evidence for nucleosome stabilization by H2Bub1 via preventing the constant H2A-H2B eviction. Recent data has also uncovered a "docking-site" on H2B for Set1-COMPASS. Collectively, these findings invoke a model, where ubiquitin acts as a "glue" to bind the nucleosome together for supporting Set1-COMPASS/Dot1 functions. This review provides an overview of these novel findings. Additionally, how H2Bub1 and its deubiquitination might alter the chromatin dynamics during transcription is discussed. Possible models for nucleosome stabilization by ubiquitin are also provided.

Indexed as

Chromatin Assembly and DisassemblyGenomic InstabilityHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansMethylationModels, BiologicalModels, MolecularNucleosomesProtein Processing, Post-TranslationalUbiquitinationHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesNucleosomes

Identifiers

PMID20523115
PMCPMC3230548
OpenAlexW2040080051

What OpenQuestion holds

Textmetadata
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.