Evidence map›Paper›PMID 22231427›Full record

ArticleNature neuroscience2012

NAB-1 instructs synapse assembly by linking adhesion molecules and F-actin to active zone proteins.

Poh Hui Chia, Maulik R Patel, Kang Shen

Open access · greenAbstract read
In one paragraph

Article in Nature neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.3field-weighted citation impact, top 6% 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, 104 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. The actin assembly regulatorbioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Presynaptic Cytomatrix Proteins.Advances in neurobiology · 2023
    Article
  17. Review
  18. Article
  19. Article
  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

3 authors at 3 institutions in 1 country.

Poh Hui ChiaHoward Hughes Medical Institute, Department of Biology, Stanford University, Stanford, California, USA.
Maulik R Patel
Kang Shen
Fred Hutch Cancer Center · USHoward Hughes Medical Institute · USStanford University · US

Funding

Mechanisms of Synaptic Specificity in C. elegansR01NS048392 · NINDS · STANFORD UNIVERSITY · PI SHEN, KANG · 2005 to 2014
$3.1M
Mechanisms of synaptic specificity in C. elegansR37NS048392 · NINDS · STANFORD UNIVERSITY · PI SHEN, KANG · 2015 to 2019
$2.0M
Howard Hughes Medical InstituteNINDS NIH HHS R01 NS048392NINDS NIH HHS R37 NS048392
6 · The paper itself

Abstract

During synaptogenesis, macromolecular protein complexes assemble at the pre- and postsynaptic membrane. Extensive literature identifies many transmembrane molecules sufficient to induce synapse formation and several intracellular scaffolding molecules responsible for assembling active zones and recruiting synaptic vesicles. However, little is known about the molecular mechanisms coupling membrane receptors to active zone molecules during development. Using Caenorhabditis elegans, we identify an F-actin network present at nascent presynaptic terminals and required for presynaptic assembly. We unravel a sequence of events whereby specificity-determining adhesion molecules define the location of developing synapses and locally assemble F-actin. Next, the adaptor protein NAB-1 (neurabin) binds to F-actin and recruits active zone proteins SYD-1 and SYD-2 (liprin-α) by forming a tripartite complex. NAB-1 localizes transiently to synapses during development and is required for presynaptic assembly. Altogether, we identify a role for the actin cytoskeleton during presynaptic development and characterize a molecular pathway whereby NAB-1 links synaptic partner recognition to active zone assembly.

Indexed as

ActinsAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansCaenorhabditis elegans ProteinsCell Adhesion MoleculesCell MovementGene Expression Regulation, DevelopmentalImmunoglobulinsIntercellular Signaling Peptides and ProteinsLarvaLuminescent ProteinsMicrofilament ProteinsMotor NeuronsMutationNerve Tissue ProteinsActinsCaenorhabditis elegans ProteinsCell Adhesion MoleculesImmunoglobulinsIntercellular Signaling Peptides and ProteinsLuminescent ProteinsMicrofilament ProteinsNerve Tissue ProteinsNeurabinsPhosphoproteinsSYD-1 protein, C elegansSYD-2 protein, C elegansSYG-1 protein, C elegans

Identifiers

PMID22231427
PMCPMC3848868
OpenAlexW2092171405

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.