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
2015
Functional Chimeras of GLIC Obtained by Adding the Intracellular Domain of Anion- and Cation-Conducting Cys-Loop Receptors
Mnatsakanyan N, Nishtala SN, Pandhare A, Fiori MC, Goyal R, Pauwels JE, Navetta AF, Ahrorov A, Jansen M. Functional Chimeras of GLIC Obtained by Adding the Intracellular Domain of Anion- and Cation-Conducting Cys-Loop Receptors. Biochemistry 2015, 54: 2670-2682. PMID: 25861708, PMCID: PMC4414916, DOI: 10.1021/acs.biochem.5b00203.Peer-Reviewed Original ResearchConceptsPentameric ligand-gated ion channelsEukaryotic pentameric ligand-gated ion channelsProkaryotic pentameric ligand-gated ion channelsIntracellular domainCys-loop receptorsComplete intracellular domainLarge intracellular domainLigand-gated ion channelsAcetylcholine-binding proteinLarge-scale expressionChaperone protein RIC-3Eukaryotic membersStructural studiesTorpedo nicotinic acetylcholine receptorSequence conservationFunctional chimerasTransmembrane domainRIC-3Eukaryotic channelsSuperfamily membersPentameric assemblyDiverse rolesProton-gated channelsOverall structural featuresNicotinic acetylcholine receptors
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