Evidence map›Paper›PMID 15964792›Full record

ArticleMolecular and cellular biology2005

Subunits of the heterotrimeric transcription factor NF-Y are imported into the nucleus by distinct pathways involving importin beta and importin 13.

Joerg Kahle, Matthias Baake, Detlef Doenecke, Werner Albig

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
–field-weighted citation impact
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

78 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. The Nuclear Transcription FactorInternational journal of molecular sciences · 2025
    Article
  6. Genome Editing of thePlants (Basel, Switzerland) · 2025
    Article
  7. Article
  8. Article
  9. Genomic identification of theMolecular breeding : new strategies in plant improvement · 2025
    Article
  10. Review
  11. Article
  12. Nuclear factor Y-A3b binds to theHorticulture research · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Characterization of Chromatin Accessibility in Fetal Bovine Chondrocytes.Animals : an open access journal from MDPI · 2023
    Article
  18. Article
  19. Article
  20. Article

18 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.

Joerg KahleInstitut für Biochemie und Molekulare Zellbiologie, Abteilung Molekularbiologie, Universität Göttingen, Humboldtallee 23, 37073 Göttingen, Germany.
Matthias Baake
Detlef Doenecke
Werner Albig

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transcriptional activator NF-Y is a heterotrimeric complex composed of NF-YA, NF-YB, and NF-YC, which specifically binds the CCAAT consensus present in about 30% of eukaryotic promoters. All three subunits contain evolutionarily conserved core regions, which comprise a histone fold motif (HFM) in the case of NF-YB and NF-YC. Our results of in vitro binding studies and nuclear import assays reveal two different transport mechanisms for NF-Y subunits. While NF-YA is imported by an importin beta-mediated pathway, the NF-YB/NF-YC heterodimer is translocated into the nucleus in an importin 13-dependent manner. We define a nonclassical nuclear localization signal (ncNLS) in NF-YA, and mutational analysis indicates that positively charged amino acid residues in the ncNLS are required for nuclear targeting of NF-YA. Importin beta binding is restricted to the monomeric, uncomplexed NF-YA subunit. In contrast, the nuclear import of NF-YB and NF-YC requires dimer formation. Only the NF-YB/NF-YC dimer, but not the monomeric components, are recognized by importin 13 and are imported into the nucleus. Importin 13 competes with NF-YA for binding to the NF-YB/NF-YC dimer. Our data suggest that a distinct binding platform derived from the HFM of both subunits, NF-YB/NF-YC, mediates those interactions.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsbeta KaryopherinsBinding, CompetitiveCCAAT-Binding FactorCell NucleusConserved SequenceDimerizationFemaleGlutathione TransferaseHeLa CellsHumansKaryopherinsMicroinjectionsMolecular Sequence Databeta KaryopherinsCCAAT-Binding FactorGlutathione TransferaseKaryopherinsProtein SubunitsRecombinant Fusion ProteinsTNPO1 protein, human

Identifiers

PMID15964792
PMCPMC1157003

What OpenQuestion holds

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Registered trials

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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.