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Structural basis for excitatory neuropeptide signaling

Rapid signaling between neurons is mediated by ligand-gated ion channels, cell-surface proteins with an extracellular ligand-binding domain and a membrane-spanning ion channel domain. The degenerin/epithelial sodium channel (DEG/ENaC) superfamily is diverse in terms of its gating stimuli, with some...

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Main Authors: Kalienkova, Valeria (Author) , Dandamudi, Mowgli (Author) , Batista Paulino, Cristina (Author) , Lynagh, Timothy (Author)
Format: Article (Journal)
Language:English
Published: 09 February 2024
In: Nature structural & molecular biology
Year: 2024, Volume: 31, Issue: 4, Pages: 717-726, [1-19]
ISSN:1545-9985
DOI:10.1038/s41594-023-01198-y
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41594-023-01198-y
Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41594-023-01198-y
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Author Notes:Valeria Kalienkova, Mowgli Dandamudi, Cristina Paulino & Timothy Lynagh

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520 |a Rapid signaling between neurons is mediated by ligand-gated ion channels, cell-surface proteins with an extracellular ligand-binding domain and a membrane-spanning ion channel domain. The degenerin/epithelial sodium channel (DEG/ENaC) superfamily is diverse in terms of its gating stimuli, with some DEG/ENaCs gated by neuropeptides, and others gated by pH, mechanical force or enzymatic activity. The mechanism by which ligands bind to and activate DEG/ENaCs is poorly understood. Here we dissected the structural basis for neuropeptide-gated activity of a neuropeptide-gated DEG/ENaC, FMRFamide-gated sodium channel 1 (FaNaC1) from the annelid worm Malacoceros fuliginosus, using cryo-electron microscopy. Structures of FaNaC1 in the ligand-free resting state and in several ligand-bound states reveal the ligand-binding site and capture the ligand-induced conformational changes of channel gating, which we verified with complementary mutagenesis experiments. Our results illuminate channel gating in DEG/ENaCs and offer a structural template for experimental dissection of channel pharmacology and ion conduction. 
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