Evidence map›Paper›PMID 18596237›Full record

ArticleMolecular biology of the cell2008

Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate nuclear pore assembly.

Beth A Rasala, Corinne Ramos, Amnon Harel, Douglass J Forbes

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

107 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  4. Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. eLife · 2023
    Article
  17. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  18. Review
  19. Article
  20. Article

47 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 2 countries.

Beth A RasalaDivision of Biological Sciences, University of California, San Diego, La Jolla, CA 92093-0347, USA.
Corinne Ramos
Amnon Harel
Douglass J Forbes
University of California San Diego · USTechnion – Israel Institute of Technology · IL

Funding

FUNCTIONAL STUDY OF NATIVE AND SYNTHETIC NUCLEIR01GM033279 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI FORBES, DOUGLASS JANE · 1985 to 2015
$7.0M
NIGMS NIH HHS R01 GM033279NIGMS NIH HHS R01 GM33279
6 · The paper itself

Abstract

Assembly of the nuclear pore, gateway to the genome, from its component subunits is a complex process. In higher eukaryotes, nuclear pore assembly begins with the binding of ELYS/MEL-28 to chromatin and recruitment of the large critical Nup107-160 pore subunit. The choreography of steps that follow is largely speculative. Here, we set out to molecularly define early steps in nuclear pore assembly, beginning with chromatin binding. Point mutation analysis indicates that pore assembly is exquisitely sensitive to the change of only two amino acids in the AT-hook motif of ELYS. The dependence on AT-rich chromatin for ELYS binding is borne out by the use of two DNA-binding antibiotics. AT-binding Distamycin A largely blocks nuclear pore assembly, whereas GC-binding Chromomycin A(3) does not. Next, we find that recruitment of vesicles containing the key integral membrane pore proteins POM121 and NDC1 to the forming nucleus is dependent on chromatin-bound ELYS/Nup107-160 complex, whereas recruitment of gp210 vesicles is not. Indeed, we reveal an interaction between the cytoplasmic domain of POM121 and the Nup107-160 complex. Our data thus suggest an order for nuclear pore assembly of 1) AT-rich chromatin sites, 2) ELYS, 3) the Nup107-160 complex, and 4) POM121- and NDC1-containing membrane vesicles and/or sheets, followed by (5) assembly of the bulk of the remaining soluble pore subunits.

Indexed as

Cell NucleusChromatinChromomycin A3DNADNA-Binding ProteinsDNA Mutational AnalysisHumansMembrane GlycoproteinsNuclear PoreNuclear Pore Complex ProteinsPoint MutationSaccharomyces cerevisiaeSchizosaccharomycesS PhaseTranscription FactorsXenopus ProteinsAHCTF1 protein, XenopusChromatinChromomycin A3DNADNA-Binding ProteinsMembrane GlycoproteinsNDC1 protein, XenopusNuclear Pore Complex ProteinsNUP107 protein, humanPOM121 protein, humanTranscription FactorsXenopus Proteins

Identifiers

PMID18596237
PMCPMC2526682
OpenAlexW2009405737

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.