Evidence map›Paper›PMID 14551260›Full record

ArticleMolecular biology of the cell2003

Significance of 14-3-3 self-dimerization for phosphorylation-dependent target binding.

Ying H Shen, Jakub Godlewski, Agnieszka Bronisz, Jun Zhu, Michael J Comb, Joseph Avruch, Guri Tzivion

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

59 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Translational control of innate barrier defense by the gut microbiota.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. 14-3-3ζ suppresses RANKL signaling by destabilizing TRAF6.The Journal of biological chemistry · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Genetic variation ofZhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  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

7 authors at 3 institutions in 1 country.

Ying H ShenCardiovascular Research Institute, Division of Molecular Cardiology, The Texas A&M University System Health Science Center, College of Medicine, Temple, Texas 76504, USA.
Jakub Godlewski
Agnieszka Bronisz
Jun Zhu
Michael J Comb
Joseph Avruch
Guri Tzivion
Texas A&M University System · USCell Signaling Technology (United States) · USHarvard University · US

Funding

Regulation of c-Raf-1 by Ras and Growth FactorsR01GM067134 · NIGMS · WAYNE STATE UNIVERSITY · PI TZIVION, GURI · 2003 to 2007
$1.3M
NIGMS NIH HHS R01 GM067134NIGMS NIH HHS R01GM-067134
6 · The paper itself

Abstract

14-3-3 proteins via binding serine/threonine-phosphorylated proteins regulate diverse intracellular processes in all eukaryotic organisms. Here, we examine the role of 14-3-3 self-dimerization in target binding, and in the susceptibility of 14-3-3 to undergo phosphorylation. Using a phospho-specific antibody developed against a degenerated mode-1 14-3-3 binding motif (RSxpSxP), we demonstrate that most of the 14-3-3-associated proteins in COS-7 cells are phosphorylated on sites that react with this antibody. The binding of these phosphoproteins depends on 14-3-3 dimerization, inasmuch as proteins associated in vivo with a monomeric 14-3-3 form are not recognized by the phospho-specific antibody. The role of 14-3-3 dimerization in the phosphorylation-dependent target binding is further exemplified with two well-defined 14-3-3 targets, Raf and DAF-16. Raf and DAF-16 can bind both monomeric and dimeric 14-3-3; however, whereas phosphorylation of specific Raf and DAF-16 sites is required for binding to dimeric 14-3-3, binding to monomeric 14-3-3 forms is entirely independent of Raf and DAF-16 phosphorylation. We also find that dimerization diminishes 14-3-3 susceptibility to phosphorylation. These findings establish a significant role of 14-3-3 dimerization in its ability to bind targets in a phosphorylation-dependent manner and point to a mechanism in which 14-3-3 phosphorylation and dimerization counterregulate each other.

Indexed as

Caenorhabditis elegans Proteins14-3-3 ProteinsAnimalsCells, CulturedChlorocebus aethiopsCOS CellsDimerizationForkhead Transcription FactorsHumansPhosphorylationProtein BindingProtein Structure, TertiaryProto-Oncogene Proteins c-rafSignal TransductionTranscription FactorsTyrosine 3-Monooxygenase14-3-3 ProteinsCaenorhabditis elegans Proteinsdaf-16 protein, C elegansForkhead Transcription FactorsProto-Oncogene Proteins c-rafTranscription FactorsTyrosine 3-Monooxygenase

Identifiers

PMID14551260
PMCPMC266786
OpenAlexW2163908632

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.