2021
Presynaptic Kv3 channels are required for fast and slow endocytosis of synaptic vesicles
Wu XS, Subramanian S, Zhang Y, Shi B, Xia J, Li T, Guo X, El-Hassar L, Szigeti-Buck K, Henao-Mejia J, Flavell RA, Horvath TL, Jonas EA, Kaczmarek LK, Wu LG. Presynaptic Kv3 channels are required for fast and slow endocytosis of synaptic vesicles. Neuron 2021, 109: 938-946.e5. PMID: 33508244, PMCID: PMC7979485, DOI: 10.1016/j.neuron.2021.01.006.Peer-Reviewed Original ResearchConceptsSlow endocytosisVesicle mobilizationF-actin cytoskeletonChannel mutationsPotassium channelsKv3.3 proteinsInhibits endocytosisRapid endocytosisNovel functionF-actinEndocytosisCrucial functionSynaptic vesiclesFamily channelsSynaptic transmissionDiscovery decadesMembrane potentialNeurotransmitter releaseDiverse neurological disordersIon conductanceMutationsReleasable poolMouse nerve terminalsPotassium channel mutationsPathological effects
2014
The Mitochondrial Complex V–Associated Large-Conductance Inner Membrane Current Is Regulated by Cyclosporine and Dexpramipexole
Alavian KN, Dworetzky SI, Bonanni L, Zhang P, Sacchetti S, Li H, Signore AP, Smith PJ, Gribkoff VK, Jonas EA. The Mitochondrial Complex V–Associated Large-Conductance Inner Membrane Current Is Regulated by Cyclosporine and Dexpramipexole. Molecular Pharmacology 2014, 87: 1-8. PMID: 25332381, PMCID: PMC4279080, DOI: 10.1124/mol.114.095661.Peer-Reviewed Original ResearchConceptsF1Fo-ATP synthaseInner mitochondrial membraneATP synthaseMitochondrial permeability transition poreSubmitochondrial vesiclesOligomycin sensitivity-conferring protein subunitMitochondrial membraneMitochondrial F1Fo-ATP synthaseMitochondrial matrix calciumFunctional conformational changesCellular energy productionHydrolysis of ATPPermeability transition poreC subunitIon conductanceATP/ADPProtein subunitsEnzyme complexOxidative phosphorylationConformational changesTransition poreComplex VLeak conductanceMatrix calciumEnergy production
1995
Structural Model of the Phospholamban Ion Channel Complex in Phospholipid Membranes
Arkin I, Rothman M, Ludlam C, Aimoto S, Engelman D, Rothschild K, Smith S. Structural Model of the Phospholamban Ion Channel Complex in Phospholipid Membranes. Journal Of Molecular Biology 1995, 248: 824-834. PMID: 7752243, DOI: 10.1006/jmbi.1995.0263.Peer-Reviewed Original ResearchConceptsSelective ion conductanceTransmembrane domainAmino acid residuesN-terminal 30 amino acid residuesAcid residuesCircular dichroismPentameric protein complexFull-length proteinC-terminal 22 amino acid residuesPhospholipid membranesIon channel complexTransmembrane helicesProtein complexesPhosphorylation sitesMembrane proteinsIon conductanceCarboxy terminusHelix bundleIon poreReticulum membraneInhibitory complexLong helixPentameric complexSecondary structureProtein
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