Evidence map›Paper›PMID 23485562›Full record

ArticleMolecular biology of the cell2013

Sp100A promotes chromatin decondensation at a cytomegalovirus-promoter-regulated transcription site.

Alyshia Newhart, Dmitri G Negorev, Ilona U Rafalska-Metcalf, Tian Yang, Gerd G Maul, Susan M Janicki

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Fate of Speckled Protein 100 (Sp100) During Herpesviruses Infection.Frontiers in cellular and infection microbiology · 2020
    Review
  7. Article
  8. SP100B Expression Indexed Hemorrhage in Mouse Models of Cerebral Hemorrhage.Indian journal of clinical biochemistry : IJCB · 2018
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

6 authors.

Alyshia NewhartMolecular and Cellular Oncogenesis Program, Wistar Institute, Philadelphia, PA 19104, USA.
Dmitri G Negorev
Ilona U Rafalska-Metcalf
Tian Yang
Gerd G Maul
Susan M Janicki

Funding

Tumor Microenvironment and MetastasisP30CA010815 · NCI · WISTAR INSTITUTE · PI Luis J Montaner · 1985 to 2026
$75.9M
Characterizing mechanisms of transcriptional activation using live cell imagingR01GM093000 · NIGMS · WISTAR INSTITUTE · PI JANICKI, SUSAN M · 2010 to 2014
$1.6M
NCI NIH HHS P30 CA010815NCI NIH HHS P30 CA10815NIGMS NIH HHS R01 GM093000NIGMS NIH HHS R01 GM 093000-02
6 · The paper itself

Abstract

Promyelocytic leukemia nuclear bodies (PML-NBs)/nuclear domain 10s (ND10s) are nuclear structures that contain many transcriptional and chromatin regulatory factors. One of these, Sp100, is expressed from a single-copy gene and spliced into four isoforms (A, B, C, and HMG), which differentially regulate transcription. Here we evaluate Sp100 function in single cells using an inducible cytomegalovirus-promoter-regulated transgene, visualized as a chromatinized transcription site. Sp100A is the isoform most strongly recruited to the transgene array, and it significantly increases chromatin decondensation. However, Sp100A cannot overcome Daxx- and α-thalassemia mental retardation, X-linked (ATRX)-mediated transcriptional repression, which indicates that PML-NB/ND10 factors function within a regulatory hierarchy. Sp100A increases and Sp100B, which contains a SAND domain, decreases acetyl-lysine regulatory factor levels at activated sites, suggesting that Sp100 isoforms differentially regulate transcription by modulating lysine acetylation. In contrast to Daxx, ATRX, and PML, Sp100 is recruited to activated arrays in cells expressing the herpes simplex virus type 1 E3 ubiquitin ligase, ICP0, which degrades all Sp100 isoforms except unsumoylated Sp100A. The recruitment Sp100A(K297R), which cannot be sumoylated, further suggests that sumoylation plays an important role in regulating Sp100 isoform levels at transcription sites. This study provides insight into the ways in which viruses may modulate Sp100 to promote their replication cycles.

Indexed as

Chromatin Assembly and DisassemblyPromoter Regions, GeneticAcetylationAdaptor Proteins, Signal TransducingAntigens, NuclearAutoantigensCo-Repressor ProteinsCytomegalovirusDNA HelicasesEpigenesis, GeneticHeLa CellsHumansMolecular ChaperonesNuclear ProteinsPromyelocytic Leukemia ProteinProtein IsoformsAdaptor Proteins, Signal TransducingAntigens, NuclearATRX protein, humanAutoantigensCALCOCO2 protein, humanCo-Repressor ProteinsDAXX protein, humanDNA HelicasesMolecular ChaperonesNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinProtein IsoformsSP100 protein, humanTranscription FactorsTumor Suppressor ProteinsX-linked Nuclear Protein

Identifiers

PMID23485562
PMCPMC3639056

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.