ArticleNature communications2020
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Complex biological systems analysis and deep learning for prognostic prediction of esophageal squamous cell carcinoma.iScience · 2026Article
- NALCN/Cch1 channelosome subunits originated in early eukaryotes.The Journal of general physiology · 2025Article
- Calcium Dynamics in Astrocyte-Neuron Communication from Intracellular to Extracellular Signaling.Cells · 2025Review
- A New Variant in the NALCN Channel Is Responsible for Cerebellar Ataxia and Cognitive Impairment.Genes · 2025Article
- Article
- Unplugging lateral fenestrations of NALCN reveals a hidden drug binding site within the pore region.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Contributions of the Sodium Leak Channel NALCN to Pacemaking of Medial Ventral Tegmental Area and Substantia Nigra Dopaminergic Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Structure and mechanism of NALCN-FAM155A-UNC79-UNC80 channel complex.Nature communications · 2022Article
- Architecture of the human NALCN channelosome.Cell discovery · 2022Article
- Article
- The Donnan-dominated resting state of skeletal muscle fibers contributes to resilience and longevity in dystrophic fibers.The Journal of general physiology · 2022Article
- Article
- Structures of human dual oxidase 1 complex in low-calcium and high-calcium states.Nature communications · 2021Article
- Structure of the human sodium leak channel NALCN in complex with FAM155A.Nature communications · 2020Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Resting membrane potential determines the excitability of the cell and is essential for the cellular electrical activities. The NALCN channel mediates sodium leak currents, which positively adjust resting membrane potential towards depolarization. The NALCN channel is involved in several neurological processes and has been implicated in a spectrum of neurodevelopmental diseases. Here, we report the cryo-EM structure of rat NALCN and mouse FAM155A complex to 2.7 Å resolution. The structure reveals detailed interactions between NALCN and the extracellular cysteine-rich domain of FAM155A. We find that the non-canonical architecture of NALCN selectivity filter dictates its sodium selectivity and calcium block, and that the asymmetric arrangement of two functional voltage sensors confers the modulation by membrane potential. Moreover, mutations associated with human diseases map to the domain-domain interfaces or the pore domain of NALCN, intuitively suggesting their pathological mechanisms.
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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 Socratic graph.