Evidence map›Paper›PMID 34786730›Full record

ArticleThe EMBO journal2021

UBR7 acts as a histone chaperone for post-nucleosomal histone H3.

Ann K Hogan, Kizhakke M Sathyan, Alexander B Willis, Sakshi Khurana, Shashank Srivastava, Ewelina Zasadzińska, Alexander S Lee, Aaron O Bailey, Matthew N Gaynes, Jiehuan Huang and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

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  13. UBR7 inhibits HCC tumorigenesis by targeting Keap1/Nrf2/Bach1/HK2 and glycolysis.Journal of experimental & clinical cancer research : CR · 2022
    Article
  14. Review
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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

17 authors at 4 institutions in 1 country.

Ann K HoganDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0002-8761-5854
Kizhakke M SathyanR. D. Berlin Center for Cell Analysis and Modeling, The University of Connecticut School of Medicine, Farmington, CT, USA.ORCID 0000-0001-6469-7052
Alexander B WillisDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0003-4145-5821
Sakshi KhuranaDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Shashank SrivastavaDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Ewelina ZasadzińskaDrug Substance Technologies, Process Development, Amgen Inc., Thousand Oaks, CA, USA.
Alexander S LeeDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0001-6214-1990
Aaron O BaileyDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX, USA.ORCID 0000-0001-8063-3032
Matthew N GaynesDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Jiehuan HuangDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Justin BodnerDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0001-7369-7724
Celeste D RosencranceDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Kelvin A WongDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Marc A MorganDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Kyle P EagenDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0002-2610-8664
Ali ShilatifardDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.
Daniel R FoltzDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL, USA.ORCID 0000-0001-7423-6188
Northwestern University · USAmgen (United States) · USThe University of Texas Medical Branch at Galveston · USUniversity of Connecticut · US

Funding

Chemistry of Life Processes Predoctoral Training ProgramT32GM105538 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2013 to 2022
$2.7M
Biochemical Basis of Chromatin Folding and Chromosome CondensationDP5OD024587 · OD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI EAGEN, KYLE PATRICK · 2017 to 2021
$2.0M
Histone chaperone networks for new and evicted histonesR01GM143638 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI FOLTZ, DANIEL RICHARD · 2021 to 2024
$1.5M
UBR7 is a novel chromatin directed E3 ubiquitin ligaseR21HD078946 · NICHD · UNIVERSITY OF VIRGINIA · PI FOLTZ, DANIEL RICHARD · 2014 to 2015
$421k
NICHD NIH HHS R21 HD078946NIGMS NIH HHS R01 GM143638NIGMS NIH HHS T32 GM105538NIH HHS DP5 OD024587
6 · The paper itself

Abstract

Histone chaperones modulate the stability of histones beginning from histone synthesis, through incorporation into DNA, and during recycling during transcription and replication. Following histone removal from DNA, chaperones regulate histone storage and degradation. Here, we demonstrate that UBR7 is a histone H3.1 chaperone that modulates the supply of pre-existing post-nucleosomal histone complexes. We demonstrate that UBR7 binds to post-nucleosomal H3K4me3 and H3K9me3 histones via its UBR box and PHD. UBR7 binds to the non-nucleosomal histone chaperone NASP. In the absence of UBR7, the pool of NASP-bound post-nucleosomal histones accumulate and chromatin is depleted of H3K4me3-modified histones. We propose that the interaction of UBR7 with NASP and histones opposes the histone storage functions of NASP and that UBR7 promotes reincorporation of post-nucleosomal H3 complexes.

Indexed as

AutoantigensCell LineHEK293 CellsHeLa CellsHistone CodeHistonesHumansNuclear ProteinsNucleosomesProtein DomainsUbiquitin-Protein LigasesAutoantigensHistonesNASP protein, humanNuclear ProteinsNucleosomesUbiquitin-Protein LigasesUBR7 protein, humanchaperonechromatinhistoneNASPUBR7

Identifiers

PMID34786730
PMCPMC8672181
OpenAlexW3212581815

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.