Evidence map›Paper›PMID 12323073›Full record

ArticleThe Biochemical journal2003

Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta.

Jörg Birkenfeld, Heinrich Betz, Dagmar Roth

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.6field-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

36 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. 14-3-3ε and ζ regulate neurogenesis and differentiation of neuronal progenitor cells in the developing brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  7. Redox regulation of 14-3-3ζ controls monocyte migration.Arteriosclerosis, thrombosis, and vascular biology · 2014
    Article
  8. Article
  9. Argonaute2 regulates the pancreatic β-cell secretome.Molecular & cellular proteomics : MCP · 2013
    Article
  10. Article
  11. Article
  12. Article
  13. Proteomic analysis of 14-3-3 zeta binding proteins in the mouse hippocampus.International journal of physiology, pathophysiology and pharmacology · 2012
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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.

Jörg BirkenfeldDepartment of Neurochemistry, Max-Planck-Institute for Brain Research, Deutschordenstrasse 46, 60528 Frankfurt, Germany.
Heinrich Betz
Dagmar Roth
Max Planck Institute for Brain Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins of the 14-3-3 family have been implicated in various physiological processes, and are thought to function as adaptors in various signal transduction pathways. In addition, 14-3-3 proteins may contribute to the reorganization of the actin cytoskeleton by interacting with as yet unidentified actin-binding proteins. Here we show that the 14-3-3 zeta isoform interacts with both the actin-depolymerizing factor cofilin and its regulatory kinase, LIM (Lin-11/Isl-1/Mec-3)-domain-containing protein kinase 1 (LIMK1). In both yeast two-hybrid assays and glutathione S-transferase pull-down experiments, these proteins bound efficiently to 14-3-3 zeta. Deletion analysis revealed consensus 14-3-3 binding sites on both cofilin and LIMK1. Furthermore, the C-terminal region of 14-3-3 zeta inhibited the binding of cofilin to actin in co-sedimentation experiments. Upon co-transfection into COS-7 cells, 14-3-3 zeta-specific immunoreactivity was redistributed into characteristic LIMK1-induced actin aggregations. Our data are consistent with 14-3-3-protein-induced changes to the actin cytoskeleton resulting from interactions with cofilin and/or LIMK1.

Indexed as

14-3-3 ProteinsActin Depolymerizing FactorsAnimalsBase SequenceCell LineCOS CellsDNA-Binding ProteinsDNA PrimersHumansImmunohistochemistryLim KinasesMicrofilament ProteinsProtein BindingProtein KinasesProtein Serine-Threonine KinasesRats14-3-3 ProteinsActin Depolymerizing FactorsDNA-Binding ProteinsDNA PrimersLIMK1 protein, humanLimk1 protein, ratLim KinasesMicrofilament ProteinsProtein KinasesProtein Serine-Threonine KinasesTyrosine 3-Monooxygenase

Identifiers

PMID12323073
PMCPMC1223062
OpenAlexW1998361398

What Socratic 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 Socratic graph.