2011
Random insertion of split-cans of the fluorescent protein venus into Shaker channels yields voltage sensitive probes with improved membrane localization in mammalian cells
Jin L, Baker B, Mealer R, Cohen L, Pieribone V, Pralle A, Hughes T. Random insertion of split-cans of the fluorescent protein venus into Shaker channels yields voltage sensitive probes with improved membrane localization in mammalian cells. Journal Of Neuroscience Methods 2011, 199: 1-9. PMID: 21497167, PMCID: PMC3281265, DOI: 10.1016/j.jneumeth.2011.03.028.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCell LineCell Line, TumorCell MembraneCytosolDNA Transposable ElementsFluorescent DyesHumansKidneyLuminescent ProteinsMembrane PotentialsMembrane ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceModels, MolecularMutation, MissenseNeuroblastomaPatch-Clamp TechniquesPeptide FragmentsProtein FoldingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryRecombinant Fusion ProteinsShaker Superfamily of Potassium ChannelsTransfectionConceptsShaker subunitsYellow fluorescent proteinEndoplasmic reticulumMammalian cellsNon-fluorescent halvesMisfolded monomersPlasma membrane expressionFluorescent protein VenusShaker potassium channelFluorescent protein (FP) voltage sensorsMembrane localizationPlasma membraneFluorescent proteinRandom insertionMembrane expressionSubunitsMembrane potentialIntracellular fluorescencePotassium channelsCellsFluorescent probeΔF/FVoltage sensorTetramerizationProtein
2002
Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton
Shupliakov O, Bloom O, Gustafsson JS, Kjaerulff O, Löw P, Tomilin N, Pieribone VA, Greengard P, Brodin L. Impaired recycling of synaptic vesicles after acute perturbation of the presynaptic actin cytoskeleton. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 14476-14481. PMID: 12381791, PMCID: PMC137908, DOI: 10.1073/pnas.212381799.Peer-Reviewed Original ResearchConceptsSynaptic vesicle clustersVesicle clustersSynaptic vesiclesEndocytic zonesC2 toxinClostridium botulinum C2 toxinClathrin-coated pitsSynaptic vesicle cycleSynaptic vesicle recyclingAccumulation of aggregatesRole of actinLamprey reticulospinal synapseBotulinum C2 toxinActin functionVesicle transportActin cytoskeletonCatalytic subunitVesicle cycleVesicle recyclingPlasma membraneActin filamentsImpaired recyclingReversible anchoringRecycled vesiclesS1 fragment
1999
Inhibition of neurotransmitter release in the lamprey reticulospinal synapse by antibody-mediated disruption of SNAP-25 function
Low P, Norlin T, Risinger C, Larhammar D, Pieribone V, Shupliakov O, Brodin L. Inhibition of neurotransmitter release in the lamprey reticulospinal synapse by antibody-mediated disruption of SNAP-25 function. European Journal Of Cell Biology 1999, 78: 787-793. PMID: 10604655, DOI: 10.1016/s0171-9335(99)80029-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAxonsCell MembraneImmunohistochemistryIn Situ HybridizationLampreysMembrane ProteinsMicroinjectionsMicroscopy, ElectronNerve Tissue ProteinsNeurotransmitter AgentsProtein BindingRecombinant Fusion ProteinsSpinal CordSynapsesSynaptic TransmissionSynaptic VesiclesSynaptosomal-Associated Protein 25ConceptsPlasma membraneSynaptic vesiclesSNAP-25Lamprey giant reticulospinal synapsePresynaptic plasma membraneSynaptic vesicle exocytosisLamprey reticulospinal synapseSNARE protein SNAP-25Protein SNAP-25Synaptic vesicle clustersNeurotransmitter releaseSNARE complexMolecular machineryVesicle exocytosisMembrane fusionVesicle cyclingPresynaptic microinjectionVesicle clustersSyntaxinPresynaptic membraneVesiclesElectron microscopic analysisAntibody-mediated disruptionMembraneMicroscopic analysis