Evidence map›Paper›PMID 29643390›Full record

ArticleNature communications2018

Functional crosstalk between histone H2B ubiquitylation and H2A modifications and variants.

Felix Wojcik, Geoffrey P Dann, Leslie Y Beh, Galia T Debelouchina, Raphael Hofmann, Tom W Muir

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

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  14. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023
    Review
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.

Felix WojcikDepartment of Chemistry, Princeton University, Princeton, NJ, 08544, USA.
Geoffrey P DannDepartment of Chemistry, Princeton University, Princeton, NJ, 08544, USA.
Leslie Y BehDepartment of Chemistry, Princeton University, Princeton, NJ, 08544, USA.
Galia T DebelouchinaDepartment of Chemistry, Princeton University, Princeton, NJ, 08544, USA.
Raphael HofmannDepartment of Chemistry, Princeton University, Princeton, NJ, 08544, USA.ORCID http://orcid.org/0000-0002-9769-6555
Tom W MuirDepartment of Chemistry, Princeton University, Princeton, NJ, 08544, USA. muir@princeton.edu.

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007388 · NIGMS · PRINCETON UNIVERSITY · PI CRISTEA, ILEANA M. · 1985 to 2022
$27.4M
Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
Development and Applications of 'Designer Chromatin'R01GM107047 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2013 to 2016
$1.2M
NCI NIH HHS P01 CA196539NIGMS NIH HHS R01 GM107047NIGMS NIH HHS R37 GM086868NIGMS NIH HHS T32 GM007388
6 · The paper itself

Abstract

Ubiquitylation of histone H2B at lysine residue 120 (H2BK120ub) is a prominent histone posttranslational modification (PTM) associated with the actively transcribed genome. Although H2BK120ub triggers several critical downstream histone modification pathways and changes in chromatin structure, less is known about the regulation of the ubiquitylation reaction itself, in particular with respect to the modification status of the chromatin substrate. Here we employ an unbiased library screening approach to profile the impact of pre-existing chromatin modifications on de novo ubiquitylation of H2BK120 by the cognate human E2:E3 ligase pair, UBE2A:RNF20/40. Deposition of H2BK120ub is found to be highly sensitive to PTMs on the N-terminal tail of histone H2A, a crosstalk that extends to the common histone variant H2A.Z. Based on a series of biochemical and cell-based studies, we propose that this crosstalk contributes to the spatial organization of H2BK120ub on gene bodies, and is thus important for transcriptional regulation.

Indexed as

Chromatin Assembly and DisassemblyProtein Processing, Post-TranslationalAmino Acid SequenceBinding SitesCloning, MolecularGene ExpressionHEK293 CellsHistonesHumansKineticsModels, MolecularNucleosomesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsHistonesNucleosomesProtein IsoformsRecombinant Proteins

Identifiers

PMID29643390
PMCPMC5895630

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.