ArticleThe Journal of general physiology2018
The weak voltage dependence of pannexin 1 channels can be tuned by N-terminal modifications.
Article in The Journal of general physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Article
- The C-terminal activating domain promotes pannexin 1 channel opening.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The C-terminal activating domain promotes Panx1 channel opening.bioRxiv : the preprint server for biology · 2024Article
- Cryo-EM structures of pannexin 1 and 3 reveal differences among pannexin isoforms.Nature communications · 2024Article
- Structure of human CALHM1 reveals key locations for channel regulation and blockade by ruthenium red.Nature communications · 2023Article
- Cryo-EM structure of human heptameric pannexin 2 channel.Nature communications · 2023Article
- Connexins and Pannexins: Important Players in Neurodevelopment, Neurological Diseases, and Potential Therapeutics.Biomedicines · 2022Review
- Oxidative Stress, Inflammation and Connexin Hemichannels in Muscular Dystrophies.Biomedicines · 2022Review
- On the molecular nature of large-pore channels.Journal of molecular biology · 2021Review
- Structure versus function: Are new conformations of pannexin 1 yet to be resolved?The Journal of general physiology · 2021Article
- A novel voltage-clamp/dye uptake assay reveals saturable transport of molecules through CALHM1 and connexin channels.The Journal of general physiology · 2020Article
- Article
- Cryo-EM structures of the ATP release channel pannexin 1.Nature structural & molecular biology · 2020Article
- Taking a close look at a large-pore channel.eLife · 2020Article
- The Cryo-EM structure of pannexin 1 reveals unique motifs for ion selection and inhibition.eLife · 2020Article
- A Genetic Polymorphism in theBiomolecules · 2020Article
- Article
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Authors and funding
5 authors.
Funding
Abstract
Pannexins are a family of ATP release channels important for physiological and pathological processes like blood pressure regulation, epilepsy, and neuropathic pain. To study these important channels in vitro, voltage stimulation is the most common and convenient tool, particularly for pannexin 1 (Panx1). However, whether Panx1 is a voltage-gated channel remains controversial. Here, we carefully examine the effect of N-terminal modification on voltage-dependent Panx1 channel activity. Using a whole-cell patch-clamp recording technique, we demonstrate that both human and mouse Panx1, with their nativeN termini, give rise to voltage-dependent currents, but only at membrane potentials larger than +100 mV. This weak voltage-dependent channel activity profoundly increases when a glycine-serine (GS) motif is inserted immediately after the first methionine. Single-channel recordings reveal that the addition of GS increases the channel open probability as well as the number of unitary conductance classes. We also find that insertions of other amino acid(s) at the same position mimics the effect of GS. On the other hand, tagging the N terminus with GFP abolishes voltage-dependent channel activity. Our results suggest that Panx1 is a channel with weak voltage dependence whose activity can be tuned by N-terminal modifications.
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