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 formationVesicles
2011
Massive 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 Phosphodiesterase