Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex

Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex

The NALCN channel mediates sodium leak currents, which in turn adjusts resting membrane potential and neuronal excitability. Here the authors describe a cryo-EM structure of mammalian NALCN-FAM155A channel complex, showing how selectivity filter contributes to sodium permeation and calcium block and...

Full description

Bibliographic Details
Main Authors: Yunlu Kang, Jing-Xiang Wu, Lei Chen
Format: Article
Language:English
Published: Nature Publishing Group 2020-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-20002-9
id doaj-4a01fb3b9eac4a6eaaf11895ad50315c
record_format Article
spelling doaj-4a01fb3b9eac4a6eaaf11895ad50315c2021-05-11T08:47:51ZengNature Publishing GroupNature Communications2041-17232020-12-0111111010.1038/s41467-020-20002-9Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complexYunlu Kang0Jing-Xiang Wu1Lei Chen2State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking UniversityState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking UniversityState Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Peking UniversityThe NALCN channel mediates sodium leak currents, which in turn adjusts resting membrane potential and neuronal excitability. Here the authors describe a cryo-EM structure of mammalian NALCN-FAM155A channel complex, showing how selectivity filter contributes to sodium permeation and calcium block and how the voltage sensors contribute to current modulation.https://doi.org/10.1038/s41467-020-20002-9
collection DOAJ
language English
format Article
sources DOAJ
author Yunlu Kang
Jing-Xiang Wu
Lei Chen
spellingShingle Yunlu Kang
Jing-Xiang Wu
Lei Chen
Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex
Nature Communications
author_facet Yunlu Kang
Jing-Xiang Wu
Lei Chen
author_sort Yunlu Kang
title Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex
title_short Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex
title_full Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex
title_fullStr Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex
title_full_unstemmed Structure of voltage-modulated sodium-selective NALCN-FAM155A channel complex
title_sort structure of voltage-modulated sodium-selective nalcn-fam155a channel complex
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2020-12-01
description The NALCN channel mediates sodium leak currents, which in turn adjusts resting membrane potential and neuronal excitability. Here the authors describe a cryo-EM structure of mammalian NALCN-FAM155A channel complex, showing how selectivity filter contributes to sodium permeation and calcium block and how the voltage sensors contribute to current modulation.
url https://doi.org/10.1038/s41467-020-20002-9
work_keys_str_mv AT yunlukang structureofvoltagemodulatedsodiumselectivenalcnfam155achannelcomplex
AT jingxiangwu structureofvoltagemodulatedsodiumselectivenalcnfam155achannelcomplex
AT leichen structureofvoltagemodulatedsodiumselectivenalcnfam155achannelcomplex
_version_ 1721450420142866432

Similar Items