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 ResearchConceptsSensory neuronsVoltage-sensing domainNav channelsTransmembrane proteinAccessory proteinsVoltage-gated sodium channelsCritical regulatorPore domainChannel gatingExtracellular loopToxin-mediated effectsNeuronal excitabilityPeptide toxinsProteinSodium channelsPharmacological activitiesNav1.7 functionKnottin peptidesNeuronsImportant insightsToxinSubunitsRegulatorDomainExcelsa
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
2014
Relative motions between left flipper and dorsal fin domains favour P2X4 receptor activation
Zhao W, Wang J, Ma X, Yang Y, Liu Y, Huang L, Fan Y, Cheng X, Chen H, Wang R, Yu Y. Relative motions between left flipper and dorsal fin domains favour P2X4 receptor activation. Nature Communications 2014, 5: 4189. PMID: 24943126, DOI: 10.1038/ncomms5189.Peer-Reviewed Original ResearchConceptsAllosteric changesChannel gatingLeft flipperP2X4 receptorDorsal fin domainAllosteric eventsP2X4 receptor activationPhysiological functionsResidues leadFin domainHydrophobic interactionsEssential roleExtracellular ATPFundamental processesZinc bridgesChannel activationReceptor activationDorsal finP2X receptorsReceptorsGatingDomainActivationL217V291