2019
A hydrophobic gate in the inner pore helix is the major determinant of inactivation in mechanosensitive Piezo channels
Zheng W, Gracheva EO, Bagriantsev SN. A hydrophobic gate in the inner pore helix is the major determinant of inactivation in mechanosensitive Piezo channels. ELife 2019, 8: e44003. PMID: 30628892, PMCID: PMC6349400, DOI: 10.7554/elife.44003.Peer-Reviewed Original ResearchConceptsPiezo channelsLining inner helixIon channelsMechanosensitive Piezo channelsInner pore helixImportance of inactivationMouse Piezo1Disease-causing mutationsHydrophobic gateInner helixPore helixPhysiological processesMechanism of inactivationStimulation triggersInactivationInactivation gatePiezo1Normal functionHelixHydrophobic barrierFast inactivationPhysical constrictionSecondary gateRate of inactivationMajor determinant
2018
TMEM150C/Tentonin3 Is a Regulator of Mechano-gated Ion Channels
Anderson EO, Schneider ER, Matson JD, Gracheva EO, Bagriantsev SN. TMEM150C/Tentonin3 Is a Regulator of Mechano-gated Ion Channels. Cell Reports 2018, 23: 701-708. PMID: 29669276, PMCID: PMC5929159, DOI: 10.1016/j.celrep.2018.03.094.Peer-Reviewed Original Research
2017
Molecular basis of tactile specialization in the duck bill
Schneider ER, Anderson EO, Mastrotto M, Matson JD, Schulz VP, Gallagher PG, LaMotte RH, Gracheva EO, Bagriantsev SN. Molecular basis of tactile specialization in the duck bill. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 13036-13041. PMID: 29109250, PMCID: PMC5724259, DOI: 10.1073/pnas.1708793114.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAvian ProteinsBeakChickensCloning, MolecularDucksEmbryo, NonmammalianGene ExpressionGenetic VectorsHEK293 CellsHumansIon ChannelsKineticsMechanoreceptorsMechanotransduction, CellularMicePatch-Clamp TechniquesRecombinant ProteinsRNA, Small InterferingSequence Homology, Amino AcidSpecies SpecificityTouchTouch PerceptionTrigeminal GanglionConceptsMolecular basisHeterologous expression systemSpecialist birdsMouse orthologPiezo2 ion channelsTactile specializationExpression systemDuck billMolecular characterizationIon channelsFeeding behaviorEdible matterPiezo2BirdsElectrophysiological characterizationSlow inactivation kineticsOrthologsVertebratesMechanoMechanotransductionKnockdownInactivation kineticsMurky watersHigh densityNeurons
2016
Low-cost functional plasticity of TRPV1 supports heat tolerance in squirrels and camels
Laursen WJ, Schneider ER, Merriman DK, Bagriantsev SN, Gracheva EO. Low-cost functional plasticity of TRPV1 supports heat tolerance in squirrels and camels. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 11342-11347. PMID: 27638213, PMCID: PMC5056056, DOI: 10.1073/pnas.1604269113.Peer-Reviewed Original ResearchMeSH KeywordsAfferent PathwaysAmino Acid SequenceAmino Acid SubstitutionAnimalsAnkyrin RepeatCamelusCapsaicinConserved SequenceGanglia, SpinalHEK293 CellsHot TemperatureHumansHydrogen-Ion ConcentrationIon Channel GatingMutationNeuronsSciuridaeSequence AlignmentThermotoleranceTRPV Cation ChannelsXenopusConceptsHeat toleranceCommon molecular strategyN-terminal ankyrinSingle amino acid changeSingle amino acid substitutionGround squirrelsPolymodal ion channelAmino acid changesAmino acid substitutionsRemarkable functional flexibilityFunctional conservationEcological nichesChemical cuesMammalian speciesMolecular strategiesAcid changesAcid substitutionsHeat sensitivityTransient receptor potential vanilloid 1Ion channelsOrthologsFunctional plasticitySquirrelsBactrian camelsSuch adaptation