2022
Mitochondrial ATP synthase c-subunit leak channel triggers cell death upon loss of its F1 subcomplex
Mnatsakanyan N, Park HA, Wu J, He X, Llaguno MC, Latta M, Miranda P, Murtishi B, Graham M, Weber J, Levy RJ, Pavlov EV, Jonas EA. Mitochondrial ATP synthase c-subunit leak channel triggers cell death upon loss of its F1 subcomplex. Cell Death & Differentiation 2022, 29: 1874-1887. PMID: 35322203, PMCID: PMC9433415, DOI: 10.1038/s41418-022-00972-7.Peer-Reviewed Original ResearchConceptsMitochondrial permeability transitionATP synthase c-subunitCell deathMitochondrial ATP synthaseChannel activityCellular energy productionLeak channelsVoltage-gated ion channelsF1 subcomplexATP synthaseC subunitInner membraneProkaryotic hostsCell stressPermeability transitionIon channelsGating mechanismOsmotic changesLarge conductanceC-ringChannels triggersNeuronal deathF1SubcomplexOsmotic gradient
2016
Direct interaction of the resistance to inhibitors of cholinesterase type 3 protein with the serotonin receptor type 3A intracellular domain
Nishtala SN, Mnatsakanyan N, Pandhare A, Leung C, Jansen M. Direct interaction of the resistance to inhibitors of cholinesterase type 3 protein with the serotonin receptor type 3A intracellular domain. Journal Of Neurochemistry 2016, 137: 528-538. PMID: 26875553, PMCID: PMC4860158, DOI: 10.1111/jnc.13578.Peer-Reviewed Original ResearchConceptsGloeobacter violaceus ligand-gated ion channelPentameric ligand-gated ion channelsLigand-gated ion channelsRIC-3Intracellular domainIon channelsType 3 proteinChaperone protein RIC-3Non-excitable cellsWild-type channelsTransmembrane domainProtein factorsHomologous subunitsPentameric assemblyHeteromeric pentamersChimera consistingInteraction surfaceProteinDirect interactionLaevis oocytesProtein expressionFirst experimental evidenceSpecific interactionsSurface expressionFunctional maturation
2013
Experimental determination of the vertical alignment between the second and third transmembrane segments of muscle nicotinic acetylcholine receptors
Mnatsakanyan N, Jansen M. Experimental determination of the vertical alignment between the second and third transmembrane segments of muscle nicotinic acetylcholine receptors. Journal Of Neurochemistry 2013, 125: 843-854. PMID: 23565737, PMCID: PMC3676432, DOI: 10.1111/jnc.12260.Peer-Reviewed Original ResearchConceptsLigand-gated ion channelsCys-loop receptorsGloeobacter violaceus ligand-gated ion channelNicotinic acetylcholine receptorsMuscle nAChRsCys-loop ligand-gated ion channelsIon channelsThird transmembrane segmentMuscle nicotinic acetylcholine receptorX-ray structureSame overall architectureAcetylcholine receptorsTransmembrane segmentsTransmembrane domainSegment M2Helical segmentsFunctional studiesChannel αSubunitsStructural informationReceptorsSignificant differencesNAChRsEukaryotes