2019
Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors
Sun L, Liu Y, Wang J, Huang L, Yang Y, Cheng X, Fan Y, Zhu M, Liang H, Tian Y, Wang H, Guo C, Yu Y. Altered allostery of the left flipper domain underlies the weak ATP response of rat P2X5 receptors. Journal Of Biological Chemistry 2019, 294: 19589-19603. PMID: 31727741, PMCID: PMC6926468, DOI: 10.1074/jbc.ra119.009959.Peer-Reviewed Original ResearchConceptsFuture transgenic studiesFull-length variantATP responseTransmembrane domainTransgenic studiesMammalian speciesP2X5 receptorsAllosteryPathological functionsSingle replacementSingle-channel recordingsSkeletal muscleExon 10Molecular modelingFunctional subtypesATPResiduesNervous systemP2X5ReceptorsDomainMammalsSpeciesTM2Lack of knowledge
2017
The nonproton ligand of acid-sensing ion channel 3 activates mollusk-specific FaNaC channels via a mechanism independent of the native FMRFamide peptide
Yang X, Niu Y, Liu Y, Yang Y, Wang J, Cheng X, Liang H, Wang H, Hu Y, Lu X, Zhu M, Xu T, Tian Y, Yu Y. The nonproton ligand of acid-sensing ion channel 3 activates mollusk-specific FaNaC channels via a mechanism independent of the native FMRFamide peptide. Journal Of Biological Chemistry 2017, 292: 21662-21675. PMID: 29123030, PMCID: PMC5766947, DOI: 10.1074/jbc.m117.814707.Peer-Reviewed Original ResearchConceptsDEG/ENaCDegenerin/epithelial sodium channelIon channelsAcid-sensing ion channelsMammalian acid-sensing ion channelsSodium channelsDiverse functionsKey residuesEpithelial sodium channelFMRFamide peptidesAncient featureChannel gatingActivation mechanismDistinct mechanismsSubfamiliesMammalsENaCUnitary conductancePathological processesNew insightsNonproton ligandIon selectivityEndogenous agonistSynaptic transmissionFaNaC