Evidence map›Paper›PMID 22500634›Full record

ArticleNeuron2012

14-3-3ε couples protein kinase A to semaphorin signaling and silences plexin RasGAP-mediated axonal repulsion.

Taehong Yang, Jonathan R Terman

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Disassembly of bundled F-actin and cellular remodeling via an interplay of Mical, cofilin, and F-actin crosslinkers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Article
  7. Investigating Developmental and Epileptic Encephalopathy UsingInternational journal of molecular sciences · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Semaphorins and their Signaling Mechanisms.Methods in molecular biology (Clifton, N.J.) · 2017
    Review
  14. Characterizing PKA-Mediated Phosphorylation of Plexin Using Purified Proteins.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Genetic dissection of plexin signaling in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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

2 authors at 1 institution in 1 country.

Taehong YangDepartments of Neuroscience and Pharmacology and Neuroscience Graduate Program, The University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Jonathan R Terman
The University of Texas Southwestern Medical Center · US

Funding

Molecular mechanisms of axon guidance and neural connectivityR01MH085923 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI JONATHAN R TERMAN · 2009 to 2026
$6.2M
NIMH NIH HHS MH085923NIMH NIH HHS R01 MH085923
6 · The paper itself

Abstract

The biochemical means through which multiple signaling pathways are integrated in navigating axons is poorly understood. Semaphorins are among the largest families of axon guidance cues and utilize Plexin (Plex) receptors to exert repulsive effects on axon extension. However, Semaphorin repulsion can be silenced by other distinct cues and signaling cascades, raising questions of the logic underlying these events. We now uncover a simple biochemical switch that controls Semaphorin/Plexin repulsive guidance. Plexins are Ras/Rap family GTPase activating proteins (GAPs) and we find that the PlexA GAP domain is phosphorylated by the cAMP-dependent protein kinase (PKA). This PlexA phosphorylation generates a specific binding site for 14-3-3ε, a phospho-binding protein that we find to be necessary for axon guidance. These PKA-mediated Plexin-14-3-3ε interactions prevent PlexA from interacting with its Ras family GTPase substrate and antagonize Semaphorin repulsion. Our results indicate that these interactions switch repulsion to adhesion and identify a point of convergence for multiple guidance molecules.

Indexed as

14-3-3 ProteinsAnimalsAxonsCell AdhesionCell Adhesion MoleculesCyclic AMP-Dependent Protein KinasesDrosophilaDrosophila ProteinsNerve Tissue ProteinsNeural Pathwaysras GTPase-Activating ProteinsReceptors, Cell SurfaceSecond Messenger SystemsSemaphorinsSignal Transduction14-3-3 ProteinsCell Adhesion MoleculesCyclic AMP-Dependent Protein KinasesDrosophila ProteinsNerve Tissue ProteinsplexA protein, Drosophilaplexinras GTPase-Activating ProteinsReceptors, Cell SurfaceSemaphorins

Identifiers

PMID22500634
PMCPMC3857333
OpenAlexW2084714593

What OpenQuestion holds

Textmetadata
LicenceTDM
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.