ArticleScience advances2023
Structures of wild-type and selected CMT1X mutant connexin 32 gap junction channels and hemichannels.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Quantifying electrostatic control of docking and binding energetics in functional Cx36 gap junctions.Communications biology · 2026Article
- In situ structure of the human gap junction.Science advances · 2026Article
- Molecular Modeling and Dynamics of a Complete Connexin-43 Gap Junction Channel in Various Phosphorylation States.The journal of physical chemistry. B · 2026Article
- Reversible lipid-mediated pH-gating of connexin-46/50 by cryo-EM.Nature communications · 2026Article
- Lipid dependence of connexin-32 gap junction channel conformations.Nature communications · 2025Article
- Light-controlled synthetic communication networks via paired connexon nanopores.Nature communications · 2025Article
- A fully human IgG1 antibody targeting connexin 32 extracellular domain blocks CMTX1 hemichannel dysfunction in an in vitro model.Cell communication and signaling : CCS · 2024Article
- The genetic and molecular basis of a connexin-linked skin disease.The Biochemical journal · 2024Review
- Article
- Connexin Gap Junction Channels and Hemichannels: Insights from High-Resolution Structures.Biology · 2024Review
- Cx31.1 can selectively intermix with co-expressed connexins to facilitate its assembly into gap junctions.Journal of cell science · 2024Article
- Mechanism of connexin channel inhibition by mefloquine and 2-aminoethoxydiphenyl borate.PloS one · 2024Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In myelinating Schwann cells, connection between myelin layers is mediated by gap junction channels (GJCs) formed by docked connexin 32 (Cx32) hemichannels (HCs). Mutations in Cx32 cause the X-linked Charcot-Marie-Tooth disease (CMT1X), a degenerative neuropathy without a cure. A molecular link between Cx32 dysfunction and CMT1X pathogenesis is still missing. Here, we describe the high-resolution cryo-electron cryo-myography (cryo-EM) structures of the Cx32 GJC and HC, along with two CMT1X-linked mutants, W3S and R22G. While the structures of wild-type and mutant GJCs are virtually identical, the HCs show a major difference: In the W3S and R22G mutant HCs, the amino-terminal gating helix partially occludes the pore, consistent with a diminished HC activity. Our results suggest that HC dysfunction may be involved in the pathogenesis of CMT1X.
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