Evidence map›Paper›PMID 24360965›Full record

ArticleCell reports2013

Linker Histone H1.2 cooperates with Cul4A and PAF1 to drive H4K31 ubiquitylation-mediated transactivation.

Kyunghwan Kim, Bomi Lee, Jaehoon Kim, Jongkyu Choi, Jin-Man Kim, Yue Xiong, Robert G Roeder, Woojin An

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

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  11. Review
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  13. Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021
    Review
  14. The missing linkGenes & development · 2021
    Review
  15. Article
  16. Article
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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

8 authors at 3 institutions in 1 country.

Kyunghwan KimDepartment of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Keck School of Medicine, Los Angeles, CA 90089, USA.
Bomi LeeDepartment of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Keck School of Medicine, Los Angeles, CA 90089, USA.
Jaehoon KimLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10065, USA.
Jongkyu ChoiDepartment of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Keck School of Medicine, Los Angeles, CA 90089, USA.
Jin-Man KimDepartment of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Keck School of Medicine, Los Angeles, CA 90089, USA.
Yue XiongDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
Robert G RoederLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10065, USA.
Woojin AnDepartment of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, University of Southern California, Keck School of Medicine, Los Angeles, CA 90089, USA. Electronic address: woojinan@usc.edu.
Rockefeller University · USUniversity of Southern California · USUniversity of North Carolina at Chapel Hill · US

Funding

Mechanisms of p53 target gene activation in DNA damage responsesR01CA129325 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 2007 to 2011
$4.0M
ROLE OF HISTONE H4 N-TERMINAL TAIL IN TRANSCRIPTION REGULATIONR01GM084209 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI AN, WOOJIN · 2008 to 2012
$1.8M
NCI NIH HHS CA129325NCI NIH HHS R01 CA129325NIGMS NIH HHS GM84209NIGMS NIH HHS R01 GM084209
6 · The paper itself

Abstract

Increasing evidence suggests that linker histone H1 can influence distinct cellular processes by acting as a gene-specific regulator. However, the mechanistic basis underlying such H1 specificity and whether H1 acts in concert with other chromatin-altering activities remain unclear. Here, we show that one of the H1 subtypes, H1.2, stably interacts with Cul4A E3 ubiquitin ligase and PAF1 elongation complexes and that such interaction potentiates target gene transcription via induction of H4K31 ubiquitylation, H3K4me3, and H3K79me2. H1.2, Cul4A, and PAF1 are functionally cooperative because their individual knockdown results in the loss of the corresponding histone marks and the deficiency of target gene transcription. H1.2 interacts with the serine 2-phosphorylated form of RNAPII, and we argue that it recruits the Cul4A and PAF1 complexes to target genes by bridging the interaction between the Cul4A and PAF1 complexes. These data define an expanded role for H1 in regulating gene transcription and illustrate its dependence on the elongation competence of RNAPII.

Indexed as

Transcriptional ActivationUbiquitinationCullin ProteinsGenes, DevelopmentalHeLa CellsHistonesHumansMutationNuclear ProteinsProtein BindingRNA Polymerase IITranscription Elongation, GeneticTranscription FactorsCUL4A protein, humanCullin ProteinsHistonesNuclear ProteinsPAF1 protein, humanRNA Polymerase IITranscription Factors

Identifiers

PMID24360965
PMCPMC3901356
OpenAlexW2089899188

What OpenQuestion holds

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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.