Evidence map›Paper›PMID 36805660›Full record

ArticleNature communications2023

Conformational changes in the human Cx43/GJA1 gap junction channel visualized using cryo-EM.

Hyuk-Joon Lee, Hyung Jin Cha, Hyeongseop Jeong, Seu-Na Lee, Chang-Won Lee, Minsoo Kim, Jejoong Yoo, Jae-Sung Woo

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
10.3field-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

39 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. Interactive segmentation of membrane and membrane-mimic densities in cryo-EM maps.Acta crystallographica. Section D, Structural biology · 2026
    Article
  3. Article
  4. Article
  5. Membrane-Associated Biomolecules for Synthetic Cell Signalling.Chembiochem : a European journal of chemical biology · 2026
    Review
  6. Article
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  8. COeLife · 2026
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  18. Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. 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

8 authors at 2 institutions in 1 country.

Hyuk-Joon Lee *Department of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID 0000-0001-7568-2307
Hyung Jin Cha *Department of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID 0000-0003-1476-3888
Hyeongseop Jeong *Department of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID 0000-0003-0095-3402
Seu-Na LeeDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.ORCID 0000-0001-7370-7056
Chang-Won LeeDepartment of Life Sciences, Korea University, Seoul, 02841, Korea.
Minsoo KimDepartment of Physics, Sungkyunkwan University, Suwon, 16419, Korea.
Jejoong YooDepartment of Physics, Sungkyunkwan University, Suwon, 16419, Korea.
Jae-Sung WooDepartment of Life Sciences, Korea University, Seoul, 02841, Korea. jaesungwoo@korea.ac.kr.ORCID 0000-0001-9163-3433
Korea University · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Connexin family proteins assemble into hexameric hemichannels in the cell membrane. The hemichannels dock together between two adjacent membranes to form gap junction intercellular channels (GJIChs). We report the cryo-electron microscopy structures of Cx43 GJICh, revealing the dynamic equilibrium state of various channel conformations in detergents and lipid nanodiscs. We identify three different N-terminal helix conformations of Cx43-gate-covering (GCN), pore-lining (PLN), and flexible intermediate (FIN)-that are randomly distributed in purified GJICh particles. The conformational equilibrium shifts to GCN by cholesteryl hemisuccinates and to PLN by C-terminal truncations and at varying pH. While GJIChs that mainly comprise GCN protomers are occluded by lipids, those containing conformationally heterogeneous protomers show markedly different pore sizes. We observe an α-to-π-helix transition in the first transmembrane helix, which creates a side opening to the membrane in the FIN and PLN conformations. This study provides basic structural information to understand the mechanisms of action and regulation of Cx43 GJICh.

Indexed as

Connexin 43Ion ChannelsCryoelectron MicroscopyGap JunctionsHumansProtein SubunitsConnexin 43GJA1 protein, humanIon ChannelsProtein Subunits

Identifiers

PMID36805660
PMCPMC9938869
OpenAlexW4321328182

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.