ArticleThe Journal of physiology2013
Kv3 channel assembly, trafficking and activity are regulated by zinc through different binding sites.
Article in The Journal of physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Identification, structural, and biophysical characterization of a positive modulator of human Kv3.1 channels.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain.Nature communications · 2022Article
- Kv3 Channels: Enablers of Rapid Firing, Neurotransmitter Release, and Neuronal Endurance.Physiological reviews · 2017Review
- Polarity of varicosity initiation in central neuron mechanosensation.The Journal of cell biology · 2017Article
- TRPM2 ion channels regulate macrophage polarization and gastric inflammation during Helicobacter pylori infection.Mucosal immunology · 2017Article
- Suppression of Inflammatory Demyelinaton and Axon Degeneration through Inhibiting Kv3 Channels.Frontiers in molecular neuroscience · 2017Article
- Differential regulation of ASICs and TRPV1 by zinc in rat bronchopulmonary sensory neurons.Lung · 2014Article
- Endogenous zinc depresses GABAergic transmission via T-type Ca(2+) channels and broadens the time window for integration of glutamatergic inputs in dentate granule cells.The Journal of physiology · 2014Article
- Astrocytes differentially respond to inflammatory autoimmune insults and imbalances of neural activity.Acta neuropathologica communications · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Zinc, a divalent heavy metal ion and an essential mineral for life, regulates synaptic transmission and neuronal excitability via ion channels. However, its binding sites and regulatory mechanisms are poorly understood. Here, we report that Kv3 channel assembly, localization and activity are regulated by zinc through different binding sites. Local perfusion of zinc reversibly reduced spiking frequency of cultured neurons most likely by suppressing Kv3 channels. Indeed, zinc inhibited Kv3.1 channel activity and slowed activation kinetics, independent of its site in the N-terminal T1 domain. Biochemical assays surprisingly identified a novel zinc-binding site in the Kv3.1 C-terminus, critical for channel activity and axonal targeting, but not for the zinc inhibition. Finally, mutagenesis revealed an important role of the junction between the first transmembrane (TM) segment and the first extracellular loop in sensing zinc. Its mutant enabled fast spiking with relative resistance to the zinc inhibition. Therefore, our studies provide novel mechanistic insights into the multifaceted regulation of Kv3 channel activity and localization by divalent heavy metal ions.
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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.