Evidence map›Paper›PMID 21289084›Full record

ArticleMolecular biology of the cell2011

Coilin participates in the suppression of RNA polymerase I in response to cisplatin-induced DNA damage.

Andrew S Gilder, Phi M Do, Zunamys I Carrero, Angela M Cosman, Hanna J Broome, Venkatramreddy Velma, Luis A Martinez, Michael D Hebert

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2011. 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
2.4field-weighted citation impact, top 11% 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, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Female Aging Affects Coilin Pattern in Mouse Cumulus Cells.Journal of developmental biology · 2026
    Article
  5. Review
  6. Article
  7. Review
  8. Roles of NOLC1 in cancers and viral infection.Journal of cancer research and clinical oncology · 2023
    Review
  9. Review
  10. Article
  11. Article
  12. Nuclear Organization in Response to Stress: A Special Focus on Nucleoli.Results and problems in cell differentiation · 2022
    Article
  13. Article
  14. Alteration of 28S rRNA 2'-Biology open · 2019
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

8 authors at 1 institution in 1 country.

Andrew S GilderDepartment of Biochemistry, University of Mississippi Medical Center, Jackson, MS 39216, USA.
Phi M Do
Zunamys I Carrero
Angela M Cosman
Hanna J Broome
Venkatramreddy Velma
Luis A Martinez
Michael D Hebert
University of Mississippi Medical Center · US

Funding

Nuclear bodies and ribonucleoprotein biogenesisR01GM081448 · NIGMS · UNIVERSITY OF MISSISSIPPI MED CTR · PI HEBERT, MICHAEL D · 2008 to 2012
$1.5M
NIGMS NIH HHS R01 GM081448NIGMS NIH HHS R01-GM-081448
6 · The paper itself

Abstract

Coilin is a nuclear phosphoprotein that concentrates within Cajal bodies (CBs) and impacts small nuclear ribonucleoprotein (snRNP) biogenesis. Cisplatin and γ-irradiation, which cause distinct types of DNA damage, both trigger the nucleolar accumulation of coilin, and this temporally coincides with the repression of RNA polymerase I (Pol I) activity. Knockdown of endogenous coilin partially overrides the Pol I transcriptional arrest caused by cisplatin, while both ectopically expressed and exogenous coilin accumulate in the nucleolus and suppress rRNA synthesis. In support of this mechanism, we demonstrate that both cisplatin and γ-irradiation induce the colocalization of coilin with RPA-194 (the largest subunit of Pol I), and we further show that coilin can specifically interact with RPA-194 and the key regulator of Pol I activity, upstream binding factor (UBF). Using chromatin immunoprecipitation analysis, we provide evidence that coilin modulates the association of Pol I with ribosomal DNA. Collectively, our data suggest that coilin acts to repress Pol I activity in response to cisplatin-induced DNA damage. Our findings identify a novel and unexpected function for coilin, independent of its role in snRNP biogenesis, establishing a new link between the DNA damage response and the inhibition of rRNA synthesis.

Indexed as

DNA DamageAntineoplastic AgentsCell LineCell NucleusChromosomal Proteins, Non-HistoneCisplatinCoiled BodiesDNADNA, RibosomalHumansNuclear ProteinsPhosphoproteinsPol1 Transcription Initiation Complex ProteinsRecombinant Fusion ProteinsReplication Protein ARNA Polymerase IAntineoplastic AgentsChromosomal Proteins, Non-HistoneCisplatinDNADNA, RibosomalfibrillarinNOLC1 protein, humanNuclear Proteinsp80-coilinPhosphoproteinsPol1 Transcription Initiation Complex ProteinsRecombinant Fusion ProteinsReplication Protein ARNA Polymerase IRNA, Ribosomaltranscription factor UBF

Identifiers

PMID21289084
PMCPMC3069010
OpenAlexW2152156251

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.