Evidence map›Paper›PMID 36906653›Full record

ArticleNature communications2023

Cryo-EM structures of human Cx36/GJD2 neuronal gap junction channel.

Seu-Na Lee, Hwa-Jin Cho, Hyeongseop Jeong, Bumhan Ryu, Hyuk-Joon Lee, Minsoo Kim, Jejoong Yoo, Jae-Sung Woo, Hyung Ho Lee

Open access · goldFull text 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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

28 citing papers in PubMed, 48 citations in OpenAlex.

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  3. COeLife · 2026
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  13. 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
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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

9 authors at 5 institutions in 2 countries.

Seu-Na Lee *Department of Life Sciences, Korea University, Seoul, 02841, Republic of Korea.ORCID 0000-0001-7370-7056
Hwa-Jin Cho *Department of Chemistry, College of Natural Sciences, Seoul National University, Seoul, 08826, Korea.
Hyeongseop JeongCenter for Research Equipment, Korea Basic Science Institute, Chungcheongbuk-do, 28119, Korea.ORCID 0000-0003-0095-3402
Bumhan RyuResearch Solution Center, Institute for Basic Science, Daejeon, 34126, Republic of Korea.
Hyuk-Joon LeeDepartment of Life Sciences, Korea University, Seoul, 02841, Republic of Korea.ORCID 0000-0001-7568-2307
Minsoo KimDepartment of Physics, Sungkyunkwan University, Suwon, 16419, South Korea.
Jejoong YooDepartment of Physics, Sungkyunkwan University, Suwon, 16419, South Korea.
Jae-Sung WooDepartment of Life Sciences, Korea University, Seoul, 02841, Republic of Korea. jaesungwoo@korea.ac.kr.ORCID 0000-0001-9163-3433
Hyung Ho LeeDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul, 08826, Korea. hyungholee@snu.ac.kr.ORCID 0000-0003-1168-2484
Korea University · KRSeoul National University · KRSungkyunkwan University · KRInstitute for Basic Science · KRKorea Basic Science Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Connexin 36 (Cx36) is responsible for signal transmission in electrical synapses by forming interneuronal gap junctions. Despite the critical role of Cx36 in normal brain function, the molecular architecture of the Cx36 gap junction channel (GJC) is unknown. Here, we determine cryo-electron microscopy structures of Cx36 GJC at 2.2-3.6 Å resolutions, revealing a dynamic equilibrium between its closed and open states. In the closed state, channel pores are obstructed by lipids, while N-terminal helices (NTHs) are excluded from the pore. In the open state with pore-lining NTHs, the pore is more acidic than those in Cx26 and Cx46/50 GJCs, explaining its strong cation selectivity. The conformational change during channel opening also includes the α-to-π-helix transition of the first transmembrane helix, which weakens the protomer-protomer interaction. Our structural analyses provide high resolution information on the conformational flexibility of Cx36 GJC and suggest a potential role of lipids in the channel gating.

Indexed as

ConnexinsElectrical SynapsesConnexin 26Cryoelectron MicroscopyGap Junction delta-2 ProteinGap JunctionsHumansIon ChannelsLipidsProtein SubunitsConnexin 26ConnexinsGap Junction delta-2 ProteinGJB2 protein, humanIon ChannelsLipidsProtein Subunits

Identifiers

PMID36906653
PMCPMC10008584
OpenAlexW4323923746

What OpenQuestion holds

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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.