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
2020
Structural and Pharmacological Characterization of the Mitochondrial Permeability Transition Pore: A Megachannel Formed by F1FO ATP Synthase
Mnatsakanyan N, Llaguno M, Yang Y, Yan Y, Weber J, Sigworth F, Jonas E. Structural and Pharmacological Characterization of the Mitochondrial Permeability Transition Pore: A Megachannel Formed by F1FO ATP Synthase. Biophysical Journal 2020, 118: 1a. DOI: 10.1016/j.bpj.2019.11.198.Peer-Reviewed Original Research
2019
A mitochondrial megachannel resides in monomeric F1FO ATP synthase
Mnatsakanyan N, Llaguno MC, Yang Y, Yan Y, Weber J, Sigworth FJ, Jonas EA. A mitochondrial megachannel resides in monomeric F1FO ATP synthase. Nature Communications 2019, 10: 5823. PMID: 31862883, PMCID: PMC6925261, DOI: 10.1038/s41467-019-13766-2.Peer-Reviewed Original ResearchConceptsATP synthase monomersMitochondrial permeability transition poreATP synthaseGiant unilamellar vesiclesMitochondrial megachannelOligomeric stateSmall unilamellar vesiclesF1Fo-ATP synthaseMitochondrial ATP synthaseMitochondrial inner membraneCryo-EM density mapsPermeability transition porePorcine heart mitochondriaUnilamellar vesiclesInner membraneMPTP activityTransition poreElectron cryomicroscopyChannel activityLipid compositionDimer formationHeart mitochondriaSynthaseChannel formationVesiclesP4‐512: EXCITOTOXIC NEURONAL DEATH INDUCING MEGACHANNEL RESIDES IN MONOMERIC F1FO ATP SYNTHASE
Mnatsakanyan N, Llaguno M, Yang Y, Yan Y, Sigworth F, Jonas E. P4‐512: EXCITOTOXIC NEURONAL DEATH INDUCING MEGACHANNEL RESIDES IN MONOMERIC F1FO ATP SYNTHASE. Alzheimer's & Dementia 2019, 15: p1509-p1510. DOI: 10.1016/j.jalz.2019.08.058.Peer-Reviewed Original ResearchMitochondrial Megachannel Resides in Monomeric ATP Synthase
Mnatsakanyan N, Park H, Jing W, Llaguno M, Murtishi B, Latta M, Davis E, Miranda P, Yang Y, Sigworth F, Jonas E. Mitochondrial Megachannel Resides in Monomeric ATP Synthase. Biophysical Journal 2019, 116: 156a. DOI: 10.1016/j.bpj.2018.11.863.Peer-Reviewed Original Research
2017
Placing and shaping liposomes with reconfigurable DNA nanocages
Zhang Z, Yang Y, Pincet F, Llaguno M, Lin C. Placing and shaping liposomes with reconfigurable DNA nanocages. Nature Chemistry 2017, 9: 653-659. PMID: 28644472, PMCID: PMC5542812, DOI: 10.1038/nchem.2802.Peer-Reviewed Original ResearchConceptsMembrane-bound vesiclesDNA cagesRegulated deformationsDNA nanocagesMembrane curvatureMembrane fusionConformational changesBiological membranesCell membraneLipid bilayer membranesMembrane mechanicsVesiclesDiverse structuresMembraneCellsBilayer membranesVersatile toolDelivery vesiclesToroid shapeLiposome shape
2016
bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles
Zheng H, Lee S, Llaguno M, Jiang Q. bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles. Journal Of Cell Biology 2016, 212: 2122oia1. DOI: 10.1083/jcb.2122oia1.Peer-Reviewed Original Research
2015
bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles
Zheng H, Lee S, Llaguno MC, Jiang QX. bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles. The Journal Of General Physiology 2015, 147: 77-93. PMID: 26712851, PMCID: PMC4692488, DOI: 10.1085/jgp.201511448.Peer-Reviewed Original ResearchConceptsMembrane proteinsIon channelsLipid compositionLipid bilayersMembrane systemLipid-protein interactionsVitro membrane systemSingle-molecule imagingVoltage-gated ion channelsGiant vesiclesUnilamellar naturePlanar electrodesPlanar lipid bilayersSuch proteinsMicroscopic imagingBiophysical analysisFast gating kineticsUnidirectional insertionProteinChannel activityProtein orientationGating kineticsModel systemBilayersSpecific ligandsStructural Studies of IP3R by Cryoem
Jiang Q, Zheng H, Llaguno M. Structural Studies of IP3R by Cryoem. Biophysical Journal 2015, 108: 340a-341a. DOI: 10.1016/j.bpj.2014.11.1866.Peer-Reviewed Original Research
2014
Chemically functionalized carbon films for single molecule imaging
Llaguno MC, Xu H, Shi L, Huang N, Zhang H, Liu Q, Jiang QX. Chemically functionalized carbon films for single molecule imaging. Journal Of Structural Biology 2014, 185: 405-417. PMID: 24457027, PMCID: PMC3990355, DOI: 10.1016/j.jsb.2014.01.006.Peer-Reviewed Original ResearchConceptsCarbon surfaceNanometer-thick carbon filmsBiological complexesCarbon filmsIndividual macromolecular complexesFunctionalized filmsBioactive ligandsChemical linkageSingle-molecule imagingSubnanogram levelActive siteStrong oxidationNanomolar levelsDNA/RNAMolecule imagingNegative-stain EMElectron microscopic imagingSelective enrichmentComplexesLigandsMacromolecular complexesFilmsProtein GSubnanomolar concentrationsLong-term storageA New Supported Membrane System for Studying the Lipid Effects on a Kv Channel
Zheng H, Lee S, Llaguno M, Zhu M, Hilgemann D, Jiang Q. A New Supported Membrane System for Studying the Lipid Effects on a Kv Channel. Biophysical Journal 2014, 106: 298a. DOI: 10.1016/j.bpj.2013.11.1735.Peer-Reviewed Original Research
2013
A Buttressed Unilamellar Membrane System for Studying Lipid-Protein Interactions
Lee S, Llaguno M, Jiang Q. A Buttressed Unilamellar Membrane System for Studying Lipid-Protein Interactions. Biophysical Journal 2013, 104: 593a-594a. DOI: 10.1016/j.bpj.2012.11.3297.Peer-Reviewed Original Research
2012
Phase transitions in the assembly of multivalent signalling proteins
Li P, Banjade S, Cheng HC, Kim S, Chen B, Guo L, Llaguno M, Hollingsworth JV, King DS, Banani SF, Russo PS, Jiang QX, Nixon BT, Rosen MK. Phase transitions in the assembly of multivalent signalling proteins. Nature 2012, 483: 336-340. PMID: 22398450, PMCID: PMC3343696, DOI: 10.1038/nature10879.Peer-Reviewed Original ResearchMeSH KeywordsActin-Related Protein 2-3 ComplexAdaptor Proteins, Signal TransducingBinding SitesBiopolymersFluorescence Recovery After PhotobleachingHeLa CellsHumansLigandsMembrane ProteinsMultiprotein ComplexesOncogene ProteinsPhase TransitionPhosphorylationProline-Rich Protein DomainsProtein Structure, QuaternaryProteinsSignal TransductionSrc Homology DomainsWiskott-Aldrich Syndrome Protein, NeuronalFunctionalized Ultrathin Carbon Films for Imaging Low-Abundance Biological Complexes
Llaguno M, Xu H, Shi L, Huang N, Zhang H, Liu Q, Jiang Q. Functionalized Ultrathin Carbon Films for Imaging Low-Abundance Biological Complexes. Biophysical Journal 2012, 102: 394a. DOI: 10.1016/j.bpj.2011.11.2151.Peer-Reviewed Original Research
2011
HaloTag® Protein-Mediated Live Cell Imaging with Bigger FluoroNanogold™
Joshi V, Jain M, Furuya F, Powell R, Hainfeld J, Llaguno M, Hilgemann D. HaloTag® Protein-Mediated Live Cell Imaging with Bigger FluoroNanogold™. Microscopy And Microanalysis 2011, 17: 150-151. DOI: 10.1017/s1431927611001620.Peer-Reviewed Original ResearchMassive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains
Fine M, Llaguno M, Lariccia V, Lin M, Yaradanakul A, Hilgemann D. Massive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains. The Journal Of General Physiology 2011, 137: 607-607. PMCID: PMC3105520, DOI: 10.1085/jgp.2010104691376c.Peer-Reviewed Original ResearchMassive calcium–activated endocytosis without involvement of classical endocytic proteins
Lariccia V, Fine M, Magi S, Lin M, Yaradanakul A, Llaguno M, Hilgemann D. Massive calcium–activated endocytosis without involvement of classical endocytic proteins. The Journal Of General Physiology 2011, 137: 605-605. PMCID: PMC3105511, DOI: 10.1085/jgp.2010104681376c.Peer-Reviewed Original ResearchMassive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains
Fine M, Llaguno MC, Lariccia V, Lin MJ, Yaradanakul A, Hilgemann DW. Massive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains. The Journal Of General Physiology 2011, 137: 137-154. PMID: 21242300, PMCID: PMC3032378, DOI: 10.1085/jgp.201010469.Peer-Reviewed Original ResearchConceptsMassive endocytosisPlasma membraneBaby hamster kidneyFM 4HEK293 cellsActin cytoskeleton remodelingNonionic detergentMembrane rufflesProtein cyclingCytoskeleton remodelingMembrane recyclingCytoplasmic sideNa/Ca exchangerTriphosphate hydrolysisCytoplasmic ATPEndocytosisMembrane monolayersCell surfaceLipid domainsG protein cyclingOuter monolayerMembrane tracerVesiclesAmphipathic drugsNP-40
2010
Massive calcium–activated endocytosis without involvement of classical endocytic proteins
Lariccia V, Fine M, Magi S, Lin MJ, Yaradanakul A, Llaguno MC, Hilgemann DW. Massive calcium–activated endocytosis without involvement of classical endocytic proteins. The Journal Of General Physiology 2010, 137: 111-132. PMID: 21187336, PMCID: PMC3010057, DOI: 10.1085/jgp.201010468.Peer-Reviewed Original ResearchActin CytoskeletonAdenosine TriphosphateAnimalsBeta-CyclodextrinsCalcineurinCalciumCell MembraneCells, CulturedCeramidesCholesterolClathrinCricetinaeDynaminsElectric CapacitanceEndocytosisEstrenesExocytosisGuanosine 5'-O-(3-Thiotriphosphate)HEK293 CellsHumansInositol Polyphosphate 5-PhosphatasesKidneyLipidsMembrane ProteinsNaphthalenesPhosphoric Monoester HydrolasesPolyaminesPyridinium CompoundsPyronesPyrrolidinonesQuaternary Ammonium CompoundsSodium-Calcium ExchangerSphingomyelin PhosphodiesteraseMassive Endocytosis Activated by Perturbing the Outer Plasmalemmal Monolayer
Fine M, Llaguno M, Yaradanakul A, Lariccia V, Magi S, Lin M, Hilgemann D. Massive Endocytosis Activated by Perturbing the Outer Plasmalemmal Monolayer. Biophysical Journal 2010, 98: 502a. DOI: 10.1016/j.bpj.2009.12.2735.Peer-Reviewed Original Research