Evidence map›Paper›PMID 14612406›Full record

ArticleMolecular and cellular biology2003

The dynamic mobility of histone H1 is regulated by cyclin/CDK phosphorylation.

Alejandro Contreras, Tracy K Hale, David L Stenoien, Jeffrey M Rosen, Michael A Mancini, Rafael E Herrera

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

74 citing papers in PubMed, 155 citations in OpenAlex.

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  14. Emergence of chromatin hierarchical loops from protein disorder and nucleosome asymmetry.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  17. Highly disordered histone H1-DNA model complexes and their condensates.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
  19. Article
  20. Article

14 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

6 authors at 1 institution in 1 country.

Alejandro ContrerasDepartment of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Tracy K Hale
David L Stenoien
Jeffrey M Rosen
Michael A Mancini
Rafael E Herrera
Baylor College of Medicine · US

Funding

Initiative for Maximizing Student Development (IMSD) ProgramR25GM056929 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI PEREIRA, FRED A · 1998 to 2023
$12.4M
MALAT1 lncRNA as a Therapeutic Target in Triple Negative Breast CancerR01CA016303 · NCI · BAYLOR COLLEGE OF MEDICINE · PI ROSEN, JEFFREY MARK · 1985 to 2022
$8.1M
NCI NIH HHS R01 CA016303NCI NIH HHS R01-CA16303-27NIGMS NIH HHS R25 GM056929
6 · The paper itself

Abstract

The linker histone H1 is involved in maintaining higher-order chromatin structures and displays dynamic nuclear mobility, which may be regulated by posttranslational modifications. To analyze the effect of H1 tail phosphorylation on the modulation of the histone's nuclear dynamics, we generated a mutant histone H1, referred to as M1-5, in which the five cyclin-dependent kinase phosphorylation consensus sites were mutated from serine or threonine residues into alanines. Cyclin E/CDK2 or cyclin A/CDK2 cannot phosphorylate the mutant in vitro. Using the technique of fluorescence recovery after photobleaching, we observed that the mobility of a green fluorescent protein (GFP)-M1-5 fusion protein is decreased compared to that of a GFP-wild-type H1 fusion protein. In addition, recovery of H1 correlated with CDK2 activity, as GFP-H1 mobility was decreased in cells with low CDK2 activity. Blocking the activity of CDK2 by p21 expression decreased the mobility of GFP-H1 but not that of GFP-M1-5. Finally, the level and rate of recovery of cyan fluorescent protein (CFP)-M1-5 were lower than those of CFP-H1 specifically in heterochromatic regions. These data suggest that CDK2 phosphorylates histone H1 in vivo, resulting in a more open chromatin structure by destabilizing H1-chromatin interactions.

Indexed as

Binding SitesCDC2-CDC28 KinasesCell LineCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclin ECyclinsGreen Fluorescent ProteinsHeLa CellsHeterochromatinHistonesHumansLuminescent ProteinsMutagenesis, Site-DirectedPhosphorylationCDC2-CDC28 KinasesCDK2 protein, humanCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclin ECyclinsGreen Fluorescent ProteinsHeterochromatinHistonesLuminescent ProteinsRecombinant Fusion Proteins

Identifiers

PMID14612406
PMCPMC262667
OpenAlexW2084634779

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.