Evidence map›Paper›PMID 18665226›Full record

ArticlePloS one2008

The N-terminal domain of the Drosophila retinoblastoma protein Rbf1 interacts with ORC and associates with chromatin in an E2F independent manner.

Joseph Ahlander, Xiao-Bo Chen, Giovanni Bosco

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Identification of E2F target genes that are rate limiting for dE2F1-dependent cell proliferation.Developmental dynamics : an official publication of the American Association of Anatomists · 2012
    Article
  6. Newly identified aspects of tumor suppression by RB.Disease models & mechanisms · 2011
    Review
  7. Article
  8. Article
  9. Article
  10. The RB/E2F pathway and regulation of RNA processing.Biochemical and biophysical research communications · 2009
    Review
  11. Sqd interacts with the Drosophila retinoblastoma tumor suppressor Rbf.Biochemical and biophysical research communications · 2009
    Article
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

Joseph AhlanderDepartment of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona, United States of America.
Xiao-Bo Chen
Giovanni Bosco
University of Arizona · US

Funding

Developmental control of replication by Drosophila RBR01GM069462 · NIGMS · UNIVERSITY OF ARIZONA · PI BOSCO, GIOVANNI · 2004 to 2012
$2.5M
NIGMS NIH HHS GM069462NIGMS NIH HHS R01 GM069462
6 · The paper itself

Abstract

backgroundThe retinoblastoma (Rb) tumor suppressor protein can function as a DNA replication inhibitor as well as a transcription factor. Regulation of DNA replication may occur through interaction of Rb with the origin recognition complex (ORC). PRINCIPAL

findingsWe characterized the interaction of Drosophila Rb, Rbf1, with ORC. Using expression of proteins in Drosophila S2 cells, we found that an N-terminal Rbf1 fragment (amino acids 1-345) is sufficient for Rbf1 association with ORC but does not bind to dE2F1. We also found that the C-terminal half of Rbf1 (amino acids 345-845) interacts with ORC. We observed that the amino-terminal domain of Rbf1 localizes to chromatin in vivo and associates with chromosomal regions implicated in replication initiation, including colocalization with Orc2 and acetylated histone H4. CONCLUSIONS/SIGNIFICANCE: Our results suggest that Rbf1 can associate with ORC and chromatin through domains independent of the E2F binding site. We infer that Rbf1 may play a role in regulating replication directly through its association with ORC and/or chromatin factors other than E2F. Our data suggest an important role for retinoblastoma family proteins in cell proliferation and tumor suppression through interaction with the replication initiation machinery.

Indexed as

AnimalsBinding SitesCell NucleusCell ProliferationChromatinDrosophilaDrosophila ProteinsE2F Transcription FactorsFluorescence Resonance Energy TransferHistonesModels, BiologicalOrigin Recognition ComplexPhotobleachingProtein BindingProtein Structure, TertiaryRetinoblastoma ProteinChromatinDrosophila ProteinsE2F Transcription FactorsHistonesOrigin Recognition ComplexRbf protein, DrosophilaRetinoblastoma ProteinTranscription Factors

Identifiers

PMID18665226
PMCPMC2475671
OpenAlexW2167813756

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.