Evidence map›Paper›PMID 18439405›Full record

ArticleNeuron2008

A presynaptic giant ankyrin stabilizes the NMJ through regulation of presynaptic microtubules and transsynaptic cell adhesion.

Jan Pielage, Ling Cheng, Richard D Fetter, Pete M Carlton, John W Sedat, Graeme W Davis

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
4.2field-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

117 citing papers in PubMed, 179 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. α-Synuclein Promotes Neuronal Dysfunction and Death by Disrupting the Binding of Ankyrin to β-Spectrin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  17. Review
  18. Article
  19. Review
  20. Review

57 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.

Jan PielageDepartment of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94158-2822, USA.
Ling Cheng
Richard D Fetter
Pete M Carlton
John W Sedat
Graeme W Davis
University of California, San Francisco · US

Funding

Molecular and Cellular Mechanisms of Synaptic GrowthR01NS047342 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DAVIS, GRAEME W · 2004 to 2012
$3.0M
TRANS-SYNAPTIC SIGNALING DURING NEUROMUSCULAR DEVELOPMENTR01NS059867 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DAVIS, GRAEME W · 2008 to 2015
$2.7M
Molecular and Cellular Mechanisms of Synaptic GrowthR37NS047342 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DAVIS, GRAEME W · 2013 to 2016
$1.4M
NINDS NIH HHS NS047342NINDS NIH HHS R01 NS047342NINDS NIH HHS R01 NS059867NINDS NIH HHS R37 NS047342
6 · The paper itself

Abstract

In a forward genetic screen for mutations that destabilize the neuromuscular junction, we identified a novel long isoform of Drosophila ankyrin2 (ank2-L). We demonstrate that loss of presynaptic Ank2-L not only causes synapse disassembly and retraction but also disrupts neuronal excitability and NMJ morphology. We provide genetic evidence that ank2-L is necessary to generate the membrane constrictions that normally separate individual synaptic boutons and is necessary to achieve the normal spacing of subsynaptic protein domains, including the normal organization of synaptic cell adhesion molecules. Mechanistically, synapse organization is correlated with a lattice-like organization of Ank2-L, visualized using extended high-resolution structured-illumination microscopy. The stabilizing functions of Ank2-L can be mapped to the extended C-terminal domain that we demonstrate can directly bind and organize synaptic microtubules. We propose that a presynaptic Ank2-L lattice links synaptic membrane proteins and spectrin to the underlying microtubule cytoskeleton to organize and stabilize the presynaptic terminal.

Indexed as

Amino Acid MotifsAnimalsAnimals, Genetically ModifiedAnkyrinsCell Adhesion Molecules, NeuronalDrosophilaDrosophila ProteinsGene Expression RegulationHorseradish PeroxidaseLarvaLuminescent ProteinsMicroscopy, Electron, TransmissionMicrotubulesMutationNeuromuscular JunctionPresynaptic TerminalsAnk2 protein, DrosophilaAnkyrinsCell Adhesion Molecules, NeuronalDrosophila Proteinsfasciclin IIHorseradish PeroxidaseLuminescent ProteinsSynapsins

Identifiers

PMID18439405
PMCPMC2699047
OpenAlexW2036560723

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.