2020
Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells
Benedetti L, Marvin JS, Falahati H, Guillén-Samander A, Looger LL, De Camilli P. Optimized Vivid-derived Magnets photodimerizers for subcellular optogenetics in mammalian cells. ELife 2020, 9: e63230. PMID: 33174843, PMCID: PMC7735757, DOI: 10.7554/elife.63230.Peer-Reviewed Original ResearchConceptsProtein fusion partnersSmall subcellular volumesSubcellular optogeneticsOrganelle contactsHomodimerization interfaceProtein modulesMammalian cellsBiological processesPhysiological processesSubcellular organellesLow temperature preincubationSimultaneous photoactivationFusion partnerCell preincubationWhole cellsSubcellular volumesConcatemerizationSpatial controlSpatiotemporal confinementCellsNeurosporaOrganellesHeterodimersVIVIDProtein
2004
Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking
Paolo G, Moskowitz HS, Gipson K, Wenk MR, Voronov S, Obayashi M, Flavell R, Fitzsimonds RM, Ryan TA, Camilli P. Impaired PtdIns(4,5)P2 synthesis in nerve terminals produces defects in synaptic vesicle trafficking. Nature 2004, 431: 415-422. PMID: 15386003, DOI: 10.1038/nature02896.Peer-Reviewed Original ResearchMeSH KeywordsAction PotentialsAnimalsBiological TransportCells, CulturedClathrinElectric ConductivityEndocytosisExocytosisGene DeletionKineticsMiceMice, KnockoutNeuronsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)Presynaptic TerminalsSynaptic TransmissionSynaptic VesiclesConceptsClathrin coat dynamicsSynaptic vesicle cycleSynaptic vesicle exocytosisSynaptic vesicle traffickingSecond messenger moleculesEarly postnatal lethalityEndocytic intermediatesVesicle traffickingMembrane proteinsVesicle cycleVesicle exocytosisPostnatal lethalityCell regulationRecycling kineticsMessenger moleculesBiochemical studiesSynaptic defectsDirect interactionImportant functionsCritical roleMultiple stepsReleasable poolRegulationNerve terminalsDephosphorylation
1999
Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
Takei K, Slepnev V, Haucke V, De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nature Cell Biology 1999, 1: 33-39. PMID: 10559861, DOI: 10.1038/9004.Peer-Reviewed Original ResearchConceptsDynamin 1Functional partnershipCell-free systemAmphiphysin 1Clathrin coatDynaminAmphiphysinRing-like structurePresence of GTPSynaptic vesiclesEndocytosisNarrow tubulesLipid bilayersMorphological evidenceBilayer curvatureVesiclesSpherical liposomesPotential functionClathrinGTPDirect morphological evidenceProteinAssembles
1988
[17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins
Lohmann S, De Camilli P, Walter U. [17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins. Methods In Enzymology 1988, 159: 183-193. PMID: 2842584, DOI: 10.1016/0076-6879(88)59019-5.Peer-Reviewed Original ResearchConceptsRII subunitsCytosolic cAMP-dependent protein kinaseAdditional proteinsType II cAMP-dependent proteinCAMP-dependent protein kinaseCAMP-dependent proteinMicrotubule-associated proteinsRII overlayProtein kinaseSDS-polyacrylamide gel electrophoresisCertain proteinsNative stateProteinSteps of purificationGel electrophoresisSubunitsCellular structureAssay conditionsNonspecific interactionsRIIHigh affinityHigh enough affinityLight microscopyKinaseAffinity