Evidence map›Paper›PMID 30793190›Full record

ArticleNucleic acids research2019

Monitoring of chromatin organization in live cells by FRIC. Effects of the inner nuclear membrane protein Samp1.

Cecilia Bergqvist, Frida Niss, Ricardo A Figueroa, Marie Beckman, Danuta Maksel, Mohammed H Jafferali, Agné Kulyté, Anna-Lena Ström, Einar Hallberg

Abstract read
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In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.Cold Spring Harbor perspectives in biology · 2021
    Review
  3. Article
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

9 authors.

Cecilia BergqvistDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16B, SE-106 91 Stockholm, Sweden.
Frida NissDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16B, SE-106 91 Stockholm, Sweden.
Ricardo A FigueroaDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16B, SE-106 91 Stockholm, Sweden.
Marie BeckmanDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16B, SE-106 91 Stockholm, Sweden.
Danuta MakselMonash Molecular Crystallisation Facility (MMCF), Monash University, VIC 3800, Australia.
Mohammed H JafferaliDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16B, SE-106 91 Stockholm, Sweden.
Agné KulytéLipid laboratory, Department of Medicine, Karolinska Institutet, SE-141 57 Huddinge, Sweden.
Anna-Lena StrömDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16B, SE-106 91 Stockholm, Sweden.
Einar HallbergDepartment of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 16B, SE-106 91 Stockholm, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In most cells, transcriptionally inactive heterochromatin is preferentially localized in the nuclear periphery and transcriptionally active euchromatin is localized in the nuclear interior. Different cell types display characteristic chromatin distribution patterns, which change dramatically during cell differentiation, proliferation, senescence and different pathological conditions. Chromatin organization has been extensively studied on a cell population level, but there is a need to understand dynamic reorganization of chromatin at the single cell level, especially in live cells. We have developed a novel image analysis tool that we term Fluorescence Ratiometric Imaging of Chromatin (FRIC) to quantitatively monitor dynamic spatiotemporal distribution of euchromatin and total chromatin in live cells. A vector (pTandemH) assures stoichiometrically constant expression of the histone variants Histone 3.3 and Histone 2B, fused to EGFP and mCherry, respectively. Quantitative ratiometric (H3.3/H2B) imaging displayed a concentrated distribution of heterochromatin in the periphery of U2OS cell nuclei. As proof of concept, peripheral heterochromatin responded to experimental manipulation of histone acetylation. We also found that peripheral heterochromatin depended on the levels of the inner nuclear membrane protein Samp1, suggesting an important role in promoting peripheral heterochromatin. Taken together, FRIC is a powerful and robust new tool to study dynamic chromatin redistribution in live cells.

Indexed as

AcetylationCell LineCell NucleusChromatinEuchromatinHeterochromatinHistonesHumansMembrane ProteinsMolecular ImagingNuclear EnvelopeNuclear ProteinsProtein Processing, Post-TranslationalChromatinEuchromatinHeterochromatinHistonesMembrane ProteinsNuclear ProteinsTMEM201 protein, human

Identifiers

PMID30793190
PMCPMC6511872

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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.