Evidence map›Paper›PMID 19794415›Full record

ArticleNature2009

A secreted complement-control-related protein ensures acetylcholine receptor clustering.

Marie Gendrel, Georgia Rapti, Janet E Richmond, Jean-Louis Bessereau

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

69 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
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  3. Anthelmintic activity of crude and separated extract ofJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2024
    Article
  4. Article
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  6. Control of Synaptic Levels of Nicotinic Acetylcholine Receptor by the Sequestering Subunit Dα5 and Secreted Scaffold Protein Hig.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  7. Article
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  11. An extracellular scaffolding complex confers unusual rectification upon an ionotropic acetylcholine receptor inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  15. Review
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  20. A complement factor H homolog, heparan sulfation, and syndecan maintain inversin compartment boundaries inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article

9 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

4 authors at 2 institutions in 2 countries.

Marie GendrelENS, Biology Department, Paris, F-75005 France.
Georgia Rapti
Janet E Richmond
Jean-Louis Bessereau
Inserm · FRUniversity of Illinois Chicago · US

Funding

The role of tomosyn in synaptic transmission.R01MH073156 · NIMH · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RICHMOND, JANET E · 2006 to 2010
$2.0M
NIMH NIH HHS R01 MH073156
6 · The paper itself

Abstract

Efficient neurotransmission at chemical synapses relies on spatial congruence between the presynaptic active zone, where synaptic vesicles fuse, and the postsynaptic differentiation, where neurotransmitter receptors concentrate. Diverse molecular systems have evolved to localize receptors at synapses, but in most cases, they rely on scaffolding proteins localized below the plasma membrane. A few systems have been suggested to control the synaptic localization of neurotransmitter receptors through extracellular interactions, such as the pentraxins that bind AMPA receptors and trigger their aggregation. However, it is not yet clear whether these systems have a central role in the organization of postsynaptic domains in vivo or rather provide modulatory functions. Here we describe an extracellular scaffold that is necessary to cluster acetylcholine receptors at neuromuscular junctions in the nematode Caenorhabditis elegans. It involves the ectodomain of the previously identified transmembrane protein LEV-10 (ref. 6) and a novel extracellular protein, LEV-9. LEV-9 is secreted by the muscle cells and localizes at cholinergic neuromuscular junctions. Acetylcholine receptors, LEV-9 and LEV-10 are interdependent for proper synaptic localization and physically interact based on biochemical evidence. Notably, the function of LEV-9 relies on eight complement control protein (CCP) domains. These domains, also called 'sushi domains', are usually found in proteins regulating complement activity in the vertebrate immune system. Because the complement system does not exist in protostomes, our results suggest that some of the numerous uncharacterized CCP proteins expressed in the mammalian brain might be directly involved in the organization of the synapse, independently from immune functions.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsMembrane ProteinsMolecular Sequence DataMusclesNeuromuscular JunctionOrgan SpecificityProtein BindingProtein Structure, TertiaryProtein TransportReceptors, CholinergicViral ProteinsCaenorhabditis elegans ProteinsLEV-10 protein, C elegansLEV-9 protein, C elegansMembrane ProteinsReceptors, CholinergicViral Proteins

Identifiers

PMID19794415
OpenAlexW1999955453

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.