2023
Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function
Jami S, Deuis J, Klasfauseweh T, Cheng X, Kurdyukov S, Chung F, Okorokov A, Li S, Zhang J, Cristofori-Armstrong B, Israel M, Ju R, Robinson S, Zhao P, Ragnarsson L, Andersson Å, Tran P, Schendel V, McMahon K, Tran H, Chin Y, Zhu Y, Liu J, Crawford T, Purushothamvasan S, Habib A, Andersson D, Rash L, Wood J, Zhao J, Stehbens S, Mobli M, Leffler A, Jiang D, Cox J, Waxman S, Dib-Hajj S, Neely G, Durek T, Vetter I. Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function. Nature Communications 2023, 14: 2442. PMID: 37117223, PMCID: PMC10147923, DOI: 10.1038/s41467-023-37963-2.Peer-Reviewed Original ResearchMeSH KeywordsAustraliaNAV1.7 Voltage-Gated Sodium ChannelPainPeptidesToxins, BiologicalUrtica dioicaConceptsSensory neuronsVoltage-sensing domainNav channelsTransmembrane proteinAccessory proteinsVoltage-gated sodium channelsCritical regulatorPore domainChannel gatingExtracellular loopToxin-mediated effectsNeuronal excitabilityPeptide toxinsProteinSodium channelsPharmacological activitiesNav1.7 functionKnottin peptidesNeuronsImportant insightsToxinSubunitsRegulatorDomainExcelsa
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
2016
Exploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel*
Niu Y, Yang Y, Liu Y, Huang L, Yang X, Fan Y, Cheng X, Cao P, Hu Y, Li L, Lu X, Tian Y, Yu Y. Exploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel*. Journal Of Biological Chemistry 2016, 291: 7571-7582. PMID: 26867576, PMCID: PMC4817185, DOI: 10.1074/jbc.m115.710251.Peer-Reviewed Original Research