Evidence map›Paper›PMID 18762580›Full record

ArticleThe Journal of cell biology2008

Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1.

Yi Hao, Ian G Macara

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.8field-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

45 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Impact of Protein NLife (Basel, Switzerland) · 2023
    Review
  8. Article
  9. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. The Multifaceted Roles of RCC1 in Tumorigenesis.Frontiers in molecular biosciences · 2020
    Review
  14. The association ofJournal of Cancer · 2020
    Article
  15. Chemical Biology of Protein N-Terminal Methyltransferases.Chembiochem : a European journal of chemical biology · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

2 authors at 2 institutions in 2 countries.

Yi HaoDepartment of Cell Biology, Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908, USA.
Ian G Macara
Institute of Cell Biology · UAUniversity of Virginia · US

Funding

TRAINING IN CELL AND MOLECULAR BIOLOGYT32GM008136 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI STUKENBERG, P. TODD · 1985 to 2020
$8.5M
The RAN GTPaseR01GM050526 · NIGMS · VANDERBILT UNIVERSITY · PI MACARA, IAN G · 1994 to 2014
$4.8M
NIGMS NIH HHS GM50526NIGMS NIH HHS R01 GM050526NIGMS NIH HHS T32 GM008136
6 · The paper itself

Abstract

RCC1 is the only known exchange factor for the Ran guanosine triphosphatase and performs essential roles in nuclear transport, spindle organization, and nuclear envelope formation. RCC1 binds to chromatin through a bimodal attachment to DNA and histones, and defects in binding cause chromosome missegregation. Chromatin binding is enhanced by apo-Ran. However, the mechanism underlying this regulation has been unclear. We now demonstrate that the N-terminal tail of RCC1 is essential for association with DNA but inhibits histone binding. Apo-Ran significantly promotes RCC1 binding to both DNA and histones, and these effects are tail mediated. Using a fluorescence resonance energy transfer biosensor, we detect conformational changes in the tail of RCC1 coupled to the two binding modes and in response to interactions with Ran and importin-alpha. The biosensor also reports changes accompanying mitosis in living cells. We propose that Ran induces an allosteric conformational switch in the tail that exposes the histone-binding surface on RCC1 and facilitates association of the positively charged tail with DNA.

Indexed as

AnimalsBinding SitesCell Cycle ProteinsCell LineChromatinDNA-Binding ProteinsDogsFluorescence Resonance Energy TransferGuanine Nucleotide Exchange FactorsHistonesHumansMitosisNuclear ProteinsPhosphorylationProtein Structure, Tertiaryran GTP-Binding ProteinCell Cycle ProteinsChromatinDNA-Binding ProteinsGuanine Nucleotide Exchange FactorsHistonesNuclear Proteinsran GTP-Binding ProteinRAN protein, humanRCC1 protein, human

Identifiers

PMID18762580
PMCPMC2528582
OpenAlexW2087839363

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.