Evidence map›Paper›PMID 19435804›Full record

ArticleJournal of cell science2009

Cajal-body formation correlates with differential coilin phosphorylation in primary and transformed cell lines.

Scoty M Hearst, Andrew S Gilder, Sandeep S Negi, Misty D Davis, Eric M George, Angela A Whittom, Cory G Toyota, Alma Husedzinovic, Oliver J Gruss, Michael D Hebert

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Review
  3. A Novel Role for Coilin in Vertebrate Innate Immunity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
    Review
  10. Nuclear architecture and the structural basis of mitotic memory.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

10 authors at 3 institutions in 2 countries.

Scoty M HearstDepartment of Biochemistry, The University of Mississippi Medical Center, Jackson, MS 39216, USA.
Andrew S Gilder
Sandeep S Negi
Misty D Davis
Eric M George
Angela A Whittom
Cory G Toyota
Alma Husedzinovic
Oliver J Gruss
Michael D Hebert
Jackson Memorial Hospital · USUniversity of Mississippi Medical Center · USDKFZ-ZMBH Alliance · DE

Funding

TOUGALOO PROTEOMICSP20RR016476 · NCRR · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI SHEARER, GLEN · 2001 to 2011
$30.4M
Nuclear bodies and ribonucleoprotein biogenesisR01GM081448 · NIGMS · UNIVERSITY OF MISSISSIPPI MED CTR · PI HEBERT, MICHAEL D · 2008 to 2012
$1.5M
NCRR NIH HHS RR 016476NIGMS NIH HHS 1R01GM081448-01A1NIGMS NIH HHS R01 GM081448
6 · The paper itself

Abstract

Cajal bodies (CBs) are nuclear structures that are thought to have diverse functions, including small nuclear ribonucleoprotein (snRNP) biogenesis. The phosphorylation status of coilin, the CB marker protein, might impact CB formation. We hypothesize that primary cells, which lack CBs, contain different phosphoisoforms of coilin compared with that found in transformed cells, which have CBs. Localization, self-association and fluorescence recovery after photobleaching (FRAP) studies on coilin phosphomutants all suggest this modification impacts the function of coilin and may thus contribute towards CB formation. Two-dimensional gel electrophoresis demonstrates that coilin is hyperphosphorylated in primary cells compared with transformed cells. mRNA levels of the nuclear phosphatase PPM1G are significantly reduced in primary cells and expression of PPM1G in primary cells induces CBs. Additionally, PPM1G can dephosphorylate coilin in vitro. Surprisingly, however, expression of green fluorescent protein alone is sufficient to form CBs in primary cells. Taken together, our data support a model whereby coilin is the target of an uncharacterized signal transduction cascade that responds to the increased transcription and snRNP demands found in transformed cells.

Indexed as

Cell Line, TumorCells, CulturedAmino Acid SequenceAnimalsCoiled BodiesHumansMolecular Sequence DataNuclear ProteinsPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 2CRecombinant Fusion ProteinsSignal TransductionSurvival of Motor Neuron 1 ProteinNuclear Proteinsp80-coilinPhosphoprotein PhosphatasesPPM1G protein, humanProtein Phosphatase 2CRecombinant Fusion ProteinsSurvival of Motor Neuron 1 Protein

Identifiers

PMID19435804
PMCPMC2684838
OpenAlexW2073383145

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.