Evidence map›Paper›PMID 37535063›Full record

ArticleeLife2023

Structure of the connexin-43 gap junction channel in a putative closed state.

Chao Qi, Silvia Acosta Gutierrez, Pia Lavriha, Alaa Othman, Diego Lopez-Pigozzi, Erva Bayraktar, Dina Schuster, Paola Picotti, Nicola Zamboni, Mario Bortolozzi and 2 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.5field-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

33 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
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  7. Connexin50 hemichannels are opened by COFrontiers in physiology · 2026
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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

12 authors at 6 institutions in 7 countries.

Chao Qi *Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.ORCID 0000-0003-1277-0363
Silvia Acosta Gutierrez *Institute for the Physics of Living Systems, Institute of Structural and Molecular Biology, University College London, London, United Kingdom.
Pia LavrihaInstitute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.
Alaa OthmanInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Diego Lopez-PigozziDepartment of Physics and Astronomy "G. Galilei", University of Padova, Padua, Italy.ORCID 0000-0002-6178-5951
Erva BayraktarVeneto Institute of Molecular Medicine (VIMM), Padua, Italy.ORCID 0000-0002-9660-5535
Dina SchusterInstitute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.ORCID 0000-0001-6611-8237
Paola PicottiInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Nicola ZamboniInstitute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
Mario BortolozziDepartment of Physics and Astronomy "G. Galilei", University of Padova, Padua, Italy.ORCID 0000-0001-7198-9838
Francesco Luigi GervasioDepartment of Chemistry, University College London, London, United Kingdom.ORCID 0000-0003-4831-5039
Volodymyr M KorkhovInstitute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland.ORCID 0000-0002-0962-9433
Paul Scherrer Institute · CHETH Zurich · CHUniversity of Padua · ITInstitute for Bioengineering of Catalonia · ESUniversity of Geneva · CHVeneto Institute of Molecular Medicine · IT

Funding

Swiss National Science Foundation 184951
6 · The paper itself

Abstract

Gap junction channels (GJCs) mediate intercellular communication by connecting two neighbouring cells and enabling direct exchange of ions and small molecules. Cell coupling via connexin-43 (Cx43) GJCs is important in a wide range of cellular processes in health and disease (Churko and Laird, 2013; Liang et al., 2020; Poelzing and Rosenbaum, 2004), yet the structural basis of Cx43 function and regulation has not been determined until now. Here, we describe the structure of a human Cx43 GJC solved by cryo-EM and single particle analysis at 2.26 Å resolution. The pore region of Cx43 GJC features several lipid-like densities per Cx43 monomer, located close to a putative lateral access site at the monomer boundary. We found a previously undescribed conformation on the cytosolic side of the pore, formed by the N-terminal domain and the transmembrane helix 2 of Cx43 and stabilized by a small molecule. Structures of the Cx43 GJC and hemichannels (HCs) in nanodiscs reveal a similar gate arrangement. The features of the Cx43 GJC and HC cryo-EM maps and the channel properties revealed by molecular dynamics simulations suggest that the captured states of Cx43 are consistent with a closed state.

Indexed as

Connexin 43Gap JunctionsCell CommunicationHumansIon ChannelsConnexin 43GJA1 protein, humanIon Channelsbiochemistrychemical biologyconnexin-43cryo-EMgap junction channelhemichannelhumanmembrane proteinmolecular biophysicsstructural biologystructure

Identifiers

PMID37535063
PMCPMC10400079
OpenAlexW4377693334

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LicenceCC BY
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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.