2020
Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes
La TM, Tachibana H, Li S, Abe T, Seiriki S, Nagaoka H, Takashima E, Takeda T, Ogawa D, Makino S, Asanuma K, Watanabe M, Tian X, Ishibe S, Sakane A, Sasaki T, Wada J, Takei K, Yamada H. Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes. The FASEB Journal 2020, 34: 16449-16463. PMID: 33070431, DOI: 10.1096/fj.202001240rr.Peer-Reviewed Original ResearchConceptsDynamin 1Microtubule organizationMouse podocytesΑ-tubulinMicrotubule bundlesGlomerular podocytesEndocytic proteinsMicrotubule bundle formationStabilization of microtubulesAcetylated α-tubulinVesicle formationNocodazole resistanceImmunoelectron microscopyMicrotubulesPhysiological significanceBundle formationRat podocytes
2014
A dynamin 1-, dynamin 3- and clathrin-independent pathway of synaptic vesicle recycling mediated by bulk endocytosis
Wu Y, O'Toole ET, Girard M, Ritter B, Messa M, Liu X, McPherson PS, Ferguson SM, De Camilli P. A dynamin 1-, dynamin 3- and clathrin-independent pathway of synaptic vesicle recycling mediated by bulk endocytosis. ELife 2014, 3: e01621. PMID: 24963135, PMCID: PMC4107917, DOI: 10.7554/elife.01621.Peer-Reviewed Original ResearchConceptsClathrin-mediated endocytosisDynamin 1Bulk endosomesBulk endocytosisSynaptic vesiclesNew synaptic vesiclesClathrin-independent pathwaySynaptic vesicle recyclingSV membranesSV reformationDynamin 3Vesicle recyclingClathrinEndocytosisLarge endocytic vacuolesEndocytic vacuolesEndosomesPotent stimulationIntense synaptic activityVacuolesPathwaySynaptic activityMassive formationExocytosisBuds
2013
Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors
Park RJ, Shen H, Liu L, Liu X, Ferguson SM, De Camilli P. Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors. Journal Of Cell Science 2013, 126: 5305-5312. PMID: 24046449, PMCID: PMC3828596, DOI: 10.1242/jcs.138578.Peer-Reviewed Original ResearchConceptsDynamin 1Dynamin inhibitorTKO cellsPeripheral membrane rufflingDouble knockoutDynamin 3 geneClathrin-mediated endocytosisTriple-knockout cellsDynamin-dependent processFluid-phase endocytosisDyngo-4aMembrane fissionMembrane rufflingDKO cellsDynamin 2Knockout cellsLow-level expressionCell physiologyDynaminEndocytosisTarget effectsDKO fibroblastsGenesCellsKO fibroblasts
2012
Role of dynamin, synaptojanin, and endophilin in podocyte foot processes
Soda K, Balkin DM, Ferguson SM, Paradise S, Milosevic I, Giovedi S, Volpicelli-Daley L, Tian X, Wu Y, Ma H, Son SH, Zheng R, Moeckel G, Cremona O, Holzman LB, De Camilli P, Ishibe S. Role of dynamin, synaptojanin, and endophilin in podocyte foot processes. Journal Of Clinical Investigation 2012, 122: 4401-4411. PMID: 23187129, PMCID: PMC3533561, DOI: 10.1172/jci65289.Peer-Reviewed Original ResearchConceptsRole of dynaminNormal embryonic developmentFiltration barrierSynaptic vesicle recyclingFoot process formationKidney filtration barrierGlomerular filtration barrierNeuronal synapse developmentDynamin's roleEndophilin 3Actin cytoskeletonActin dynamicsFunctional partnersDynamin 1Endophilin-1Embryonic developmentVesicle recyclingProtein networkKidney's glomerular filtration barrierSynapse developmentDynaminPodocyte foot processesNeuronal synapsesSynaptojaninEndophilinIdentification of CSPα Clients Reveals a Role in Dynamin 1 Regulation
Zhang YQ, Henderson MX, Colangelo CM, Ginsberg SD, Bruce C, Wu T, Chandra SS. Identification of CSPα Clients Reveals a Role in Dynamin 1 Regulation. Neuron 2012, 74: 136-150. PMID: 22500636, PMCID: PMC3328141, DOI: 10.1016/j.neuron.2012.01.029.Peer-Reviewed Original ResearchConceptsProtein clientsDynamin 1T-SNARE SNAP-25Cysteine string protein αSynaptic vesicle endocytosisSynaptic vesicle fusionChaperone complexClient proteinsVesicle endocytosisSystematic proteomicsSynaptic vesicle numberSuch proteinsCSPαVesicle fusionSNAP-25Synapse maintenanceProtein αVesicle numberProteinNeuronal dysfunctionCochaperonesHsc70ProteomicsEndocytosisHippocampal cultures
2009
A possible effector role for the pleckstrin homology (PH) domain of dynamin
Bethoney KA, King MC, Hinshaw JE, Ostap EM, Lemmon MA. A possible effector role for the pleckstrin homology (PH) domain of dynamin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2009, 106: 13359-13364. PMID: 19666604, PMCID: PMC2720410, DOI: 10.1073/pnas.0906945106.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainHomology domainPH domainAbility of dynaminLarge GTPase dynaminPH domain mutationsPhosphoinositide-containing membranesGTPase dynaminDynamin functionVesicle scissionMembrane scissionDynamin helixDynamin assemblyTargeting roleDynamin oligomersDynamin 1Possible effector roleAnimal cellsBisphosphate moleculesActin polymerizationDynaminClathrinDomain mutationsPhosphoinositideEndocytosis
2000
Signal-dependent membrane targeting by pleckstrin homology (PH) domains
LEMMON M, FERGUSON K. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochemical Journal 2000, 350: 1-18. DOI: 10.1042/bj3500001.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsPleckstrin homology domainPH domainHomology domainSignal-dependent recruitmentSmall protein modulesDifferent protein ligandsMost PH domainsGreen fluorescent proteinMembrane associationProtein modulesCellular signalingDynamin 1Cytoskeletal rearrangementsCell signalingOligomeric statePlasma membraneMembrane bindingStructural basisHost proteinsFluorescent proteinProtein ligandsPhysiological functionsPhysiological roleAmino acidsPhosphoinositide
1999
The Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*
Lai M, Hong J, Ruggiero A, Burnett P, Slepnev V, De Camilli P, Snyder S. The Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*. Journal Of Biological Chemistry 1999, 274: 25963-25966. PMID: 10473536, DOI: 10.1074/jbc.274.37.25963.Peer-Reviewed Original ResearchConceptsCalcium sensorEndocytic coat proteinsSynaptic endocytic machinerySynaptic vesicle endocytosisSynaptic vesiclesCalcium-dependent phosphatase calcineurinEndocytic machineryVesicle endocytosisDynamin 1Phosphatase calcineurinCoat proteinCalcium-dependent formationCalcium-sensing mechanismPhysical associationEndocytosisVesiclesCalcium-dependent processesClathrinSynaptotagminComplexesExocytosisCalcineurinMachineryProteinFunctional 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 evidenceProteinAssemblesDominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
Lee A, Frank D, Marks M, Lemmon M. Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain. Current Biology 1999, 9: 261-265. PMID: 10074457, DOI: 10.1016/s0960-9822(99)80115-8.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainReceptor-mediated endocytosisDynamin 1Homology domainEndocytic vesiclesPH domain bindsDynamin PH domainDominant negative inhibitorHigher-order oligomersDominant-negative inhibitionDynamin functionDomain bindsDynamin oligomersGTP bindingGTP hydrolysisGTPase activityPlasma membraneDynaminEndocytosisVesiclesPhosphoinositideBindsDomainMembrane
1998
Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes
Slepnev V, Ochoa G, Butler M, Grabs D, De Camilli P. Role of Phosphorylation in Regulation of the Assembly of Endocytic Coat Complexes. Science 1998, 281: 821-824. PMID: 9694653, DOI: 10.1126/science.281.5378.821.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex beta SubunitsAdaptor Proteins, Vesicular TransportAdenosine TriphosphateAnimalsBinding SitesCarbazolesChromatography, AffinityClathrinCyclosporineDimerizationDynamin IDynaminsEndocytosisEnzyme InhibitorsGTP PhosphohydrolasesIndole AlkaloidsMembrane ProteinsNerve Tissue ProteinsPhosphoric Monoester HydrolasesRatsRecombinant Fusion Proteinssrc Homology Domains
1997
Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells
Artalejo C, Lemmon M, Schlessinger J, Palfrey H. Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells. The EMBO Journal 1997, 16: 1565-1574. PMID: 9130701, PMCID: PMC1169760, DOI: 10.1093/emboj/16.7.1565.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal MedullaAmino Acid SequenceAnimalsBlood ProteinsCattleChromaffin CellsDynamin IDynaminsEndocytosisGenetic VariationGTP PhosphohydrolasesHumansModels, StructuralMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesPhosphoproteinsPolymerase Chain ReactionProtein Structure, SecondaryRecombinant ProteinsSequence Homology, Amino AcidConceptsPH domainDynamin 1Rapid endocytosisPleckstrin homology domainAmino acidsDynamin PH domainIsolated PH domainTypes of endocytosisChromaffin cellsHomology domainDynamin 2Mutational studiesEquivalent residuesEndocytotic processDifferent isoformsAdrenal chromaffin cellsEndocytosisDynaminVariable loopScission eventsSpecific roleCellsKey roleDomainIsoforms
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