Evidence map›Paper›PMID 12529402›Full record

ArticleMolecular and cellular biology2003

Live-cell fluorescence imaging reveals the dynamics of protein kinase CK2 individual subunits.

Odile Filhol, Arsenio Nueda, Véronique Martel, Delphine Gerber-Scokaert, Maria José Benitez, Catherine Souchier, Yasmina Saoudi, Claude Cochet

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 132 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Characterization of RAGE and CK2 Expressions in Human Fetal Membranes.International journal of molecular sciences · 2023
    Article
  6. Yeast Protein Asf1 Possesses Modulating Activity towards Protein Kinase CK2.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Article
  9. Predictive functional, statistical and structural analysis ofFrontiers in molecular biosciences · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Frontiers in cellular and infection microbiology · 2019
    Article
  18. Article
  19. Review
  20. Article

1 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

8 authors at 2 institutions in 1 country.

Odile FilholINSERM EMI 104, Département Réponse et Dynamique Cellulaires, CEA, 38054 Grenoble, France.
Arsenio Nueda
Véronique Martel
Delphine Gerber-Scokaert
Maria José Benitez
Catherine Souchier
Yasmina Saoudi
Claude Cochet
Inserm · FRCEA Grenoble · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinase CK2 is a multifunctional enzyme which has long been described as a stable heterotetrameric complex resulting from the association of two catalytic (alpha or alpha') and two regulatory (beta) subunits. To track the spatiotemporal dynamics of CK2 in living cells, we fused its catalytic alpha and regulatory beta subunits with green fluorescent protein (GFP). Both CK2 subunits contain nuclear localization domains that target them independently to the nucleus. Imaging of stable cell lines expressing low levels of GFP-CK2alpha or GFP-CK2beta revealed the existence of CK2 subunit subpopulations exhibiting differential dynamics. Once in the nucleus, they diffuse randomly at different rates. Unlike CK2beta, CK2alpha can shuttle, showing the dynamic nature of the nucleocytoplasmic trafficking of the kinase. When microinjected in the cytoplasm, the isolated CK2 subunits are rapidly translocated into the nucleus, whereas the holoenzyme complex remains in this cell compartment, suggesting an intramolecular masking of the nuclear localization sequences that suppresses nuclear accumulation. However, binding of FGF-2 to the holoenzyme triggers its nuclear translocation. Since the substrate specificity of CK2alpha is dramatically changed by its association with CK2beta, the control of the nucleocytoplasmic distribution of each subunit may represent a unique potential regulatory mechanism for CK2 activity.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsCasein Kinase IICell NucleusCytoplasmGreen Fluorescent ProteinsLuminescent ProteinsMiceMicroscopy, FluorescenceModels, BiologicalNuclear Localization SignalsProtein Serine-Threonine KinasesProtein Structure, TertiaryProtein SubunitsRecombinant Fusion ProteinsCasein Kinase IIGreen Fluorescent ProteinsLuminescent ProteinsNuclear Localization SignalsProtein Serine-Threonine KinasesProtein SubunitsRecombinant Fusion Proteins

Identifiers

PMID12529402
PMCPMC140707
OpenAlexW1978265006

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.