Evidence map›Paper›PMID 29670100›Full record

ArticleNature communications2018

Structural basis of epilepsy-related ligand-receptor complex LGI1-ADAM22.

Atsushi Yamagata, Yuri Miyazaki, Norihiko Yokoi, Hideki Shigematsu, Yusuke Sato, Sakurako Goto-Ito, Asami Maeda, Teppei Goto, Makoto Sanbo, Masumi Hirabayashi and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed, 1 pooled it
4.4field-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

40 citing papers in PubMed, 1 synthesis or guideline pooled it, 100 citations in OpenAlex.

  1. Pooled it
  2. Review
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  8. Review
  9. LGI1 Autoantibodies Enhance Synaptic Transmission by Presynaptic KNeurology(R) neuroimmunology & neuroinflammation · 2024
    Article
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  16. Rescue of Normal Excitability in LGI1-Deficient Epileptic Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
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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

14 authors at 3 institutions in 2 countries.

Atsushi YamagataInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Yuri MiyazakiDivision of Membrane Physiology, Department of Molecular and Cellular Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.
Norihiko YokoiDivision of Membrane Physiology, Department of Molecular and Cellular Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.ORCID http://orcid.org/0000-0001-9141-5313
Hideki ShigematsuRIKEN Center for Life Science Technologies, Tsurumi-ku, Yokohama, 230-0045, Japan.
Yusuke SatoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Sakurako Goto-ItoInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Asami MaedaInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan.
Teppei GotoCenter for Genetic Analysis of Behavior, National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.
Makoto SanboCenter for Genetic Analysis of Behavior, National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.
Masumi HirabayashiDepartment of Physiological Sciences, School of Life Science, SOKENDAI (The Graduate University for Advanced Studies), Okazaki, 444-8787, Japan.
Mikako ShirouzuRIKEN Center for Life Science Technologies, Tsurumi-ku, Yokohama, 230-0045, Japan.
Yuko FukataDivision of Membrane Physiology, Department of Molecular and Cellular Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan.
Masaki FukataDivision of Membrane Physiology, Department of Molecular and Cellular Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, 444-8787, Japan. mfukata@nips.ac.jp.
Shuya FukaiInstitute for Quantitative Biosciences, The University of Tokyo, Tokyo, 113-0032, Japan. fukai@iam.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0002-1241-1443
National Institutes of Natural Sciences · JPJapan Synchrotron Radiation Research Institute · JPQuantitative BioSciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Epilepsy is a common brain disorder throughout history. Epilepsy-related ligand-receptor complex, LGI1-ADAM22, regulates synaptic transmission and has emerged as a determinant of brain excitability, as their mutations and acquired LGI1 autoantibodies cause epileptic disorders in human. Here, we report the crystal structure of human LGI1-ADAM22 complex, revealing a 2:2 heterotetrameric assembly. The hydrophobic pocket of the C-terminal epitempin-repeat (EPTP) domain of LGI1 binds to the metalloprotease-like domain of ADAM22. The N-terminal leucine-rich repeat and EPTP domains of LGI1 mediate the intermolecular LGI1-LGI1 interaction. A pathogenic R474Q mutation of LGI1, which does not exceptionally affect either the secretion or the ADAM22 binding, is located in the LGI1-LGI1 interface and disrupts the higher-order assembly of the LGI1-ADAM22 complex in vitro and in a mouse model for familial epilepsy. These studies support the notion that the LGI1-ADAM22 complex functions as the trans-synaptic machinery for precise synaptic transmission.

Indexed as

Synaptic TransmissionADAM ProteinsAnimalsBrainBrain DiseasesCell MembraneCryoelectron MicroscopyDimerizationDisease Models, AnimalEpilepsyHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsMiceMutationNerve Tissue ProteinsADAM22 protein, humanADAM23 protein, humanADAM ProteinsIntracellular Signaling Peptides and ProteinsLGI1 protein, humanNerve Tissue ProteinsProteins

Identifiers

PMID29670100
PMCPMC5906670
OpenAlexW2802005789

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.