Evidence map›Paper›PMID 21084592›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010

Three Drosophila liprins interact to control synapse formation.

Sergio Astigarraga, Kerstin Hofmeyer, Reza Farajian, Jessica E Treisman

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

52 citing papers in PubMed, 78 citations in OpenAlex.

  1. Liprin-α family proteins and their cellular functions.The Journal of biological chemistry · 2026
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  12. UNC-2 CaV2 Channel Localization at Presynaptic Active Zones Depends on UNC-10/RIM and SYD-2/Liprin-α inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  13. Liprin-α-Mediated Assemblies and Their Roles in Synapse Formation.Frontiers in cell and developmental biology · 2021
    Review
  14. Review
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  20. Mechanisms of PTPσ-Mediated Presynaptic Differentiation.Frontiers in synaptic neuroscience · 2019
    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

4 authors at 1 institution in 1 country.

Sergio AstigarragaKimmel Center for Biology and Medicine of the Skirball Institute and Department of Cell Biology, New York University School of Medicine, New York, New York 10016, USA.
Kerstin Hofmeyer
Reza Farajian
Jessica E Treisman
New York University · US

Funding

Mechanisms of receptor protein tyrosine phosphatase signaling in Drosophila develR01GM089799 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI TREISMAN, JESSICA E · 2010 to 2014
$1.3M
NIGMS NIH HHS GM089799NIGMS NIH HHS R01 GM089799
6 · The paper itself

Abstract

Liprin-α proteins are adaptors that interact with the receptor protein tyrosine phosphatase leukocyte common antigen-related (LAR) and other synaptic proteins to promote synaptic partner selection and active zone assembly. Liprin-β proteins bind to and share homology with Liprin-α proteins, but their functions at the synapse are unknown. The Drosophila genome encodes single Liprin-α and Liprin-β homologs, as well as a third related protein that we named Liprin-γ. We show that both Liprin-β and Liprin-γ physically interact with Liprin-α and that Liprin-γ also binds to LAR. Liprin-α mutations have been shown to disrupt synaptic target layer selection by R7 photoreceptors and to reduce the size of larval neuromuscular synapses. We have generated null mutations in Liprin-β and Liprin-γ to investigate their role in these processes. We find that, although Liprin-α mutant R7 axons terminate before reaching the correct target layer, Liprin-β mutant R7 axons grow beyond their target layer. Larval neuromuscular junction size is reduced in both Liprin-α and Liprin-β mutants, and further reduced in double mutants, suggesting independent functions for these Liprins. Genetic interactions demonstrate that both Liprin proteins act through the exchange factor Trio to promote stable target selection by R7 photoreceptor axons and growth of neuromuscular synapses. Photoreceptor and neuromuscular synapses develop normally in Liprin-γ mutants; however, removing Liprin-γ improves R7 targeting in Liprin-α mutants, and restores normal neuromuscular junction size to Liprin-β mutants, suggesting that Liprin-γ counteracts the functions of the other two Liprins. We propose that context-dependent interactions between the three Liprins modulate their functions in synapse formation.

Indexed as

AnimalsAnimals, Genetically ModifiedCarrier ProteinsCell Adhesion MoleculesCells, CulturedDrosophilaDrosophila ProteinsFemaleGene Knockdown TechniquesIntracellular Signaling Peptides and ProteinsMaleNeuromuscular JunctionPhosphoproteinsProtein BindingProtein IsoformsSynapsesCarrier ProteinsCell Adhesion MoleculesDrosophila ProteinsIntracellular Signaling Peptides and ProteinsLiprin-alpha protein, Drosophilaliprin-beta protein, Drosophilaliprin-gamma protein, DrosophilaPhosphoproteinsProtein Isoforms

Identifiers

PMID21084592
PMCPMC2999520
OpenAlexW2005089183

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.