Evidence map›Paper›PMID 18003830›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007

SynCAMs organize synapses through heterophilic adhesion.

Adam I Fogel, Michael R Akins, Alexander J Krupp, Massimiliano Stagi, Valentin Stein, Thomas Biederer

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 5% 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

121 citing papers in PubMed, 1 synthesis or guideline pooled it, 205 citations in OpenAlex.

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  20. Overlapping morphological, immunohistochemical and genetic features of superficial CD34-positive fibroblastic tumor and PRDM10-rearranged soft tissue tumor.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2022
    Article

61 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 3 institutions in 2 countries.

Adam I FogelDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
Michael R Akins
Alexander J Krupp
Massimiliano Stagi
Valentin Stein
Thomas Biederer
Yale University · USMax Planck Institute of Neurobiology · DEMax Planck Society · DE

Funding

Yale/NIDA Neuroproteomics Research CenterP30DA018343 · NIDA · YALE UNIVERSITY · PI Marina R Picciotto · 2004 to 2026
$37.1M
Mechanisms of SynCAM-Induced Synapse FormationR01DA018928 · NIDA · YALE UNIVERSITY · PI BIEDERER, THOMAS · 2005 to 2021
$4.6M
NIDA NIH HHS P30 DA018343NIDA NIH HHS R01 DA018928
6 · The paper itself

Abstract

Synapses are asymmetric cell junctions with precisely juxtaposed presynaptic and postsynaptic sides. Transsynaptic adhesion complexes are thought to organize developing synapses. The molecular composition of these complexes, however, remains incompletely understood, precluding us from understanding how adhesion across the synaptic cleft guides synapse development. Here, we define two immunoglobulin superfamily members, SynCAM 1 and 2, that are expressed in neurons in the developing brain and localize to excitatory and inhibitory synapses. They function as cell adhesion molecules and assemble with each other across the synaptic cleft into a specific, transsynaptic SynCAM 1/2 complex. Additionally, SynCAM 1 and 2 promote functional synapses as they increase the number of active presynaptic terminals and enhance excitatory neurotransmission. The interaction of SynCAM 1 and 2 is affected by glycosylation, indicating regulation of this adhesion complex by posttranslational modification. The SynCAM 1/2 complex is representative for the highly defined adhesive patterns of this protein family, the four members of which are expressed in neurons in divergent expression profiles. SynCAMs 1, 2, and 3 each can bind themselves, yet preferentially assemble into specific, heterophilic complexes as shown for the synaptic SynCAM 1/2 interaction and a second complex comprising SynCAM 3 and 4. Our results define SynCAM proteins as components of novel heterophilic transsynaptic adhesion complexes that set up asymmetric interactions, with SynCAM proteins contributing to synapse organization and function.

Indexed as

AnimalsCell AdhesionCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCell DifferentiationCell LineCells, CulturedCoculture TechniquesHippocampusHumansImmunoglobulinsMacromolecular SubstancesMiceNeural PathwaysPresynaptic TerminalsProtein IsoformsCadm1 protein, ratCell Adhesion MoleculesCell Adhesion Molecules, NeuronalImmunoglobulinsMacromolecular SubstancesProtein IsoformsTumor Suppressor Proteins

Identifiers

PMID18003830
PMCPMC6673342
OpenAlexW2126357600

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.