Evidence map›Paper›PMID 20141511›Full record

ArticleThe Biochemical journal2010

Bioinformatic and experimental survey of 14-3-3-binding sites.

Catherine Johnson, Sandra Crowther, Margaret J Stafford, David G Campbell, Rachel Toth, Carol MacKintosh

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 186 papers.

0numbers the graph read from it
0cells of the map it votes in
186citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

186 citing papers in PubMed, 357 citations in OpenAlex.

  1. Article
  2. A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  3. Review
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  7. Restoring the 14-3-3/CRAF regulatory interaction in Noonan syndrome using molecular glues.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Identification of 14-3-3 Proteins as Binding Partners of TRP Channels.Journal of chemical information and modeling · 2026
    Article
  10. Article
  11. Article
  12. Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. ProlineJournal of the American Chemical Society · 2025
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  17. Article
  18. Article
  19. Review
  20. Review

126 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

6 authors at 1 institution in 1 country.

Catherine JohnsonMRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dundee DD15EH, Scotland, U.K.
Sandra Crowther
Margaret J Stafford
David G Campbell
Rachel Toth
Carol MacKintosh
MRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Medical Research Council
6 · The paper itself

Abstract

More than 200 phosphorylated 14-3-3-binding sites in the literature were analysed to define 14-3-3 specificities, identify relevant protein kinases, and give insights into how cellular 14-3-3/phosphoprotein networks work. Mode I RXX(pS/pT)XP motifs dominate, although the +2 proline residue occurs in less than half, and LX(R/K)SX(pS/pT)XP is prominent in plant 14-3-3-binding sites. Proline at +1 is rarely reported, and such motifs did not stand up to experimental reanalysis of human Ndel1. Instead, we discovered that 14-3-3 interacts with two residues that are phosphorylated by basophilic kinases and located in the DISC1 (disrupted-in-schizophrenia 1)-interacting region of Ndel1 that is implicated in cognitive disorders. These data conform with the general findings that there are different subtypes of 14-3-3-binding sites that overlap with the specificities of different basophilic AGC (protein kinase A/protein kinase G/protein kinase C family) and CaMK (Ca2+/calmodulin-dependent protein kinase) protein kinases, and a 14-3-3 dimer often engages with two tandem phosphorylated sites, which is a configuration with special signalling, mechanical and evolutionary properties. Thus 14-3-3 dimers can be digital logic gates that integrate more than one input to generate an action, and coincidence detectors when the two binding sites are phosphorylated by different protein kinases. Paired sites are generally located within disordered regions and/or straddle either side of functional domains, indicating how 14-3-3 dimers modulate the conformations and/or interactions of their targets. Finally, 14-3-3 proteins bind to members of several multi-protein families. Two 14-3-3-binding sites are conserved across the class IIa histone deacetylases, whereas other protein families display differential regulation by 14-3-3s. We speculate that 14-3-3 dimers may have contributed to the evolution of such families, tailoring regulatory inputs to different physiological demands.

Indexed as

Computational Biology14-3-3 ProteinsBinding SitesBlotting, WesternCalcium-Calmodulin-Dependent Protein KinasesCarrier ProteinsCells, CulturedDimerizationHumansImmunoprecipitationKidneyNerve Tissue ProteinsPhosphorylationProtein BindingProtein KinasesReverse Transcriptase Polymerase Chain Reaction14-3-3 ProteinsCalcium-Calmodulin-Dependent Protein KinasesCarrier ProteinsDISC1 protein, humanNDEL1 protein, humanNerve Tissue ProteinsProtein KinasesRNA, Messenger

Identifiers

PMID20141511
PMCPMC2860806
OpenAlexW2162404348

What OpenQuestion holds

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LicenceCC BY-NC
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.