Evidence map›Paper›PMID 32324534›Full record

ArticleeLife2020

Optogenetic control of excitatory post-synaptic differentiation through neuroligin-1 tyrosine phosphorylation.

Mathieu Letellier, Matthieu Lagardère, Béatrice Tessier, Harald Janovjak, Olivier Thoumine

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  6. Cell Adhesion Molecule Signaling at the Synapse: Beyond the Scaffold.Cold Spring Harbor perspectives in biology · 2024
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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

5 authors at 2 institutions in 2 countries.

Mathieu LetellierUniversity of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France.ORCID 0000-0003-4008-298X
Matthieu LagardèreUniversity of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France.
Béatrice TessierUniversity of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France.
Harald JanovjakAustralian Regenerative Medicine Institute (ARMI), Faculty of Medicine, Nursing and Health Sciences, Monash University, Clayton, Australia.
Olivier ThoumineUniversity of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297, Bordeaux, France.ORCID 0000-0002-8041-1349
Centre National de la Recherche Scientifique · FRAustralian Regenerative Medicine Institute · AU

Funding

CEREBRAL CHEMISTRY IN DEMENTIA AND AGING--TREATMENTSZ01AG000401 · NIA · AGING · PI SHETTY, H U · 1994 to 1998
–
Agence Nationale de la Recherche ANR-17-CE16-0028-01Conseil Régional Aquitaine « SiMoDyn »Fondation pour la Recherche Médicale DEQ20160334916France BioImaging ANR-10INBS-04-01Investissements d'avenir Labex BRAIN ANR-10-LABX-43
6 · The paper itself

Abstract

Neuroligins (Nlgns) are adhesion proteins mediating trans-synaptic contacts in neurons. However, conflicting results around their role in synaptic differentiation arise from the various techniques used to manipulate Nlgn expression level. Orthogonally to these approaches, we triggered here the phosphorylation of endogenous Nlgn1 in CA1 mouse hippocampal neurons using a photoactivatable tyrosine kinase receptor (optoFGFR1). Light stimulation for 24 hr selectively increased dendritic spine density and AMPA-receptor-mediated EPSCs in wild-type neurons, but not in Nlgn1 knock-out neurons or when endogenous Nlgn1 was replaced by a non-phosphorylatable mutant (Y782F). Moreover, light stimulation of optoFGFR1 partially occluded LTP in a Nlgn1-dependent manner. Combined with computer simulations, our data support a model by which Nlgn1 tyrosine phosphorylation promotes the assembly of an excitatory post-synaptic scaffold that captures surface AMPA receptors. This optogenetic strategy highlights the impact of Nlgn1 intracellular signaling in synaptic differentiation and potentiation, while enabling an acute control of these mechanisms.

Indexed as

AnimalsCell Adhesion Molecules, NeuronalExcitatory Postsynaptic PotentialsHippocampusMembrane ProteinsNerve Tissue ProteinsNeuronsOptogeneticsPhosphorylationReceptors, AMPASynapsesTyrosineCell Adhesion Molecules, NeuronalMembrane ProteinsNerve Tissue Proteinsneuroligin 1Receptors, AMPATyrosineadhesion moleculesglutamate receptorsmouseneuroscienceoptogeneticssynapse differentiationtyrosine kinase receptors

Identifiers

PMID32324534
PMCPMC7180054
OpenAlexW3018738470

What OpenQuestion holds

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LicenceCC BY
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.