Evidence map›Paper›PMID 41329163›Full record

ArticleThe Journal of cell biology2026

GARLH regulates neuroligin preference for excitatory versus inhibitory synapses.

Tokiwa Yamasaki, Kohtarou Konno, Dilja Krueger-Burg, Yoav Noam, Nashid H Chaudhury, Megumi Morimoto-Tomita, Elizabeth J Salm, Masahiko Watanabe, Nils Brose, Susumu Tomita

Abstract read
In one paragraph

Article in The Journal of cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

10 authors.

Tokiwa Yamasaki *Department of Cellular and Molecular Physiology, Department of Neuroscience, CNNR Program, Yale University School of Medicine, New Haven, CT, USA.ORCID 0000-0001-7963-6682
Kohtarou Konno *Department of Anatomy, Faculty of Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0003-4964-8011
Dilja Krueger-BurgDepartment of Molecular Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID 0000-0001-5597-6287
Yoav NoamDepartment of Cellular and Molecular Physiology, Department of Neuroscience, CNNR Program, Yale University School of Medicine, New Haven, CT, USA.ORCID 0009-0008-4704-0153
Nashid H ChaudhuryDepartment of Cellular and Molecular Physiology, Department of Neuroscience, CNNR Program, Yale University School of Medicine, New Haven, CT, USA.ORCID 0000-0001-5531-622X
Megumi Morimoto-TomitaDepartment of Cellular and Molecular Physiology, Department of Neuroscience, CNNR Program, Yale University School of Medicine, New Haven, CT, USA.ORCID 0009-0009-5437-6824
Elizabeth J SalmDepartment of Cellular and Molecular Physiology, Department of Neuroscience, CNNR Program, Yale University School of Medicine, New Haven, CT, USA.ORCID 0000-0001-8221-7294
Masahiko WatanabeDepartment of Anatomy, Faculty of Medicine, Hokkaido University, Sapporo, Japan.ORCID 0000-0001-5037-7138
Nils BroseDepartment of Molecular Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID 0000-0003-0938-8534
Susumu TomitaDepartment of Cellular and Molecular Physiology, Department of Neuroscience, CNNR Program, Yale University School of Medicine, New Haven, CT, USA.ORCID 0000-0001-8344-259X

Funding

Mechanisms for synaptic localization of ionotropic GABA receptors in the brainR01MH115705 · NIMH · YALE UNIVERSITY · PI TOMITA, SUSUMU · 2018 to 2022
$2.1M
Bundesministerium für Bildung und ForschungDeutsche Forschungsgemeinschaft KR5239/1Deutsche Forschungsgemeinschaft SFB1286/A09National Research Service Award 1F30MH113299NIMH NIH HHS MH115705NIMH NIH HHS R01 MH115705Uehara Memorial Foundation
6 · The paper itself

Abstract

Synaptic specificity is governed by precise combinations of cell adhesion proteins that stabilize pre- and postsynaptic sites and appropriate neurotransmitter receptors. The postsynaptic neuroligins NL1/3 and NL2/3/4 localize to excitatory and inhibitory synapses, respectively, and regulate the corresponding neurotransmitter receptors. However, the exact molecular mechanisms that determine synaptic specificity via defined combinations of neuroligins and neurotransmitter receptors remain unclear. We found that all neuroligin isoforms form a tripartite complex with GABAA receptors and GARLH4 protein, with isoform-specific preferences, and that NL1, previously thought to be restricted to excitatory synapses, is also present at inhibitory synapses. In the absence of inhibitory synapse-specific NL2/4, NL1/3 increasingly assembles with GARLH4/GABAA receptors and relocates to inhibitory synapses. Moreover, forced interaction between NL1 and GARLH4 redirects their localization to inhibitory synapses. These findings demonstrate that GARLHs regulate the synaptic specificity of neuroligins, providing the key link between neuroligins and inhibitory GABAA receptors.

Indexed as

Cell Adhesion Molecules, NeuronalMembrane ProteinsNerve Tissue ProteinsSynapsesAnimalsHEK293 CellsHumansMiceNeuroliginsNeuronsProtein IsoformsReceptors, GABA-ACell Adhesion Molecules, NeuronalMembrane ProteinsNerve Tissue Proteinsneuroligin 1NeuroliginsProtein IsoformsReceptors, GABA-A

Identifiers

PMID41329163
PMCPMC13310181

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Registered trials

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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.