Evidence map›Paper›PMID 26979420›Full record

ArticleNature communications2016

Mapping the dynamics and nanoscale organization of synaptic adhesion proteins using monomeric streptavidin.

Ingrid Chamma, Mathieu Letellier, Corey Butler, Béatrice Tessier, Kok-Hong Lim, Isabel Gauthereau, Daniel Choquet, Jean-Baptiste Sibarita, Sheldon Park, Matthieu Sainlos and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
33.7field-weighted citation impact, top 1% 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

81 citing papers in PubMed, 161 citations in OpenAlex.

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21 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

11 authors at 2 institutions in 2 countries.

Ingrid ChammaInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Mathieu LetellierInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Corey ButlerInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Béatrice TessierInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Kok-Hong LimDepartment of Chemical and Biological Engineering, University at Buffalo, Buffalo, New York 14260, USA.
Isabel GauthereauInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Daniel ChoquetInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Jean-Baptiste SibaritaInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Sheldon ParkDepartment of Chemical and Biological Engineering, University at Buffalo, Buffalo, New York 14260, USA.
Matthieu SainlosInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.ORCID http://orcid.org/0000-0001-5465-5641
Olivier ThoumineInterdisciplinary Institute for Neuroscience, UMR 5297, Centre National de la Recherche Scientifique, 33077 Bordeaux, France.
Université de Bordeaux · FRUniversity at Buffalo, State University of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The advent of super-resolution imaging (SRI) has created a need for optimized labelling strategies. We present a new method relying on fluorophore-conjugated monomeric streptavidin (mSA) to label membrane proteins carrying a short, enzymatically biotinylated tag, compatible with SRI techniques including uPAINT, STED and dSTORM. We demonstrate efficient and specific labelling of target proteins in confined intercellular and organotypic tissues, with reduced steric hindrance and no crosslinking compared with multivalent probes. We use mSA to decipher the dynamics and nanoscale organization of the synaptic adhesion molecules neurexin-1β, neuroligin-1 (Nlg1) and leucine-rich-repeat transmembrane protein 2 (LRRTM2) in a dual-colour configuration with GFP nanobody, and show that these proteins are diffusionally trapped at synapses where they form apposed trans-synaptic adhesive structures. Furthermore, Nlg1 is dynamic, disperse and sensitive to synaptic stimulation, whereas LRRTM2 is organized in compact and stable nanodomains. Thus, mSA is a versatile tool to image membrane proteins at high resolution in complex live environments, providing novel information about the nano-organization of biological structures.

Indexed as

AnimalsBiotinylationCell Adhesion Molecules, NeuronalGreen Fluorescent ProteinsHEK293 CellsHippocampusHumansIndicators and ReagentsMembrane ProteinsMiceMice, KnockoutMolecular Dynamics SimulationNanotechnologyNerve Tissue ProteinsNeural Cell Adhesion MoleculesNeuronsCell Adhesion Molecules, NeuronalGreen Fluorescent ProteinsIndicators and ReagentsLRRTM2 protein, humanLRRTM2 protein, mouseLRRTM2 protein, ratMembrane ProteinsNerve Tissue ProteinsNeural Cell Adhesion Moleculesneurexin Ibetaneuroligin 1Streptavidin

Identifiers

PMID26979420
PMCPMC4799371
OpenAlexW2298172813

What OpenQuestion holds

Textmetadata
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.