ArticleNature communications2023
Structure of human CALHM1 reveals key locations for channel regulation and blockade by ruthenium red.
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 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Transient infrared laser exposure modulates calcium activity in cortical dendritic spines.Biophotonics discovery · 2026Article
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- CALHM5 deficiency alleviates aortic aneurysm by regulating smooth muscle calcium homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Lipid dependence of connexin-32 gap junction channel conformations.Nature communications · 2025Article
- ANTIDOTE: A Metadata-Driven Neural Network for Improving CryoEM 3-D Particle Sorting.bioRxiv : the preprint server for biology · 2025Article
- Identification and classification of ion-channels across the tree of life provide functional insights into understudied CALHM channels.bioRxiv : the preprint server for biology · 2025Article
- Biology, function and structure of the calcium homeostasis modulator family.The Journal of physiology · 2025Review
- Intracellular calcium imaging for agonist screening.Biophysics reports · 2025Article
- A mechanism of CALHM1 ion channel gating.American journal of physiology. Cell physiology · 2025Article
- Oligomeric rearrangement may regulate channel activity.Biophysics reports · 2024Article
- Mefloquine-induced conformational shift in Cx36 N-terminal helix leading to channel closure mediated by lipid bilayer.Nature communications · 2024Article
- Large-pore connexin hemichannels function like molecule transporters independent of ion conduction.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Cryo-EM structures of pannexin 1 and 3 reveal differences among pannexin isoforms.Nature communications · 2024Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Calcium homeostasis modulator 1 (CALHM1) is a voltage-dependent channel involved in neuromodulation and gustatory signaling. Despite recent progress in the structural biology of CALHM1, insights into functional regulation, pore architecture, and channel blockade remain limited. Here we present the cryo-EM structure of human CALHM1, revealing an octameric assembly pattern similar to the non-mammalian CALHM1s and the lipid-binding pocket conserved across species. We demonstrate by MD simulations that this pocket preferentially binds a phospholipid over cholesterol to stabilize its structure and regulate the channel activities. Finally, we show that residues in the amino-terminal helix form the channel pore that ruthenium red binds and blocks.
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Registered trials
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.