2020
Role of VPS13, a protein with similarity to ATG2, in physiology and disease
Ugur B, Hancock-Cerutti W, Leonzino M, De Camilli P. Role of VPS13, a protein with similarity to ATG2, in physiology and disease. Current Opinion In Genetics & Development 2020, 65: 61-68. PMID: 32563856, PMCID: PMC7746581, DOI: 10.1016/j.gde.2020.05.027.Peer-Reviewed Original ResearchConceptsAutophagy protein ATG2N-terminal halfVPS13 proteinsMolecular functionsCellular processesFamily proteinsVps13Contact sitesAtg2Intracellular organellesFunctional studiesNovel mechanismProteinSimilar roleHydrophobic channelStructural studiesNeurodegenerative disordersPhysiologyDirect transferOrganellesSimilarityMutationsRoleLipidsBilayers
2019
SynGO: An Evidence-Based, Expert-Curated Knowledge Base for the Synapse
Koopmans F, van Nierop P, Andres-Alonso M, Byrnes A, Cijsouw T, Coba M, Cornelisse L, Farrell R, Goldschmidt H, Howrigan D, Hussain N, Imig C, de Jong A, Jung H, Kohansalnodehi M, Kramarz B, Lipstein N, Lovering R, MacGillavry H, Mariano V, Mi H, Ninov M, Osumi-Sutherland D, Pielot R, Smalla K, Tang H, Tashman K, Toonen R, Verpelli C, Reig-Viader R, Watanabe K, van Weering J, Achsel T, Ashrafi G, Asi N, Brown T, De Camilli P, Feuermann M, Foulger R, Gaudet P, Joglekar A, Kanellopoulos A, Malenka R, Nicoll R, Pulido C, de Juan-Sanz J, Sheng M, Südhof T, Tilgner H, Bagni C, Bayés À, Biederer T, Brose N, Chua J, Dieterich D, Gundelfinger E, Hoogenraad C, Huganir R, Jahn R, Kaeser P, Kim E, Kreutz M, McPherson P, Neale B, O'Connor V, Posthuma D, Ryan T, Sala C, Feng G, Hyman S, Thomas P, Smit A, Verhage M. SynGO: An Evidence-Based, Expert-Curated Knowledge Base for the Synapse. Neuron 2019, 103: 217-234.e4. PMID: 31171447, PMCID: PMC6764089, DOI: 10.1016/j.neuron.2019.05.002.Peer-Reviewed Original Research
2017
Contacts between the endoplasmic reticulum and other membranes in neurons
Wu Y, Whiteus C, Xu CS, Hayworth KJ, Weinberg RJ, Hess HF, De Camilli P. Contacts between the endoplasmic reticulum and other membranes in neurons. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e4859-e4867. PMID: 28559323, PMCID: PMC5474793, DOI: 10.1073/pnas.1701078114.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumER–plasma membrane contactsER-PM contactsMembrane contactSmaller focal contactsRegulation of CaInterorganelle communicationOrganelle biogenesisDifferent neuronal compartmentsCell physiologyIntracellular membranesFocal contactsMultivesicular bodiesER contactsIntracellular organellesER cisternaeLipid homeostasisBiochemical studiesTubulovesicular structuresMembrane appositionNeuronal compartmentsImportant functionsMitochondriaReticulumMembrane
2001
PIP Kinase Iγ Is the Major PI(4,5)P2 Synthesizing Enzyme at the Synapse
Wenk M, Pellegrini L, Klenchin V, Di Paolo G, Chang S, Daniell L, Arioka M, Martin T, De Camilli P. PIP Kinase Iγ Is the Major PI(4,5)P2 Synthesizing Enzyme at the Synapse. Neuron 2001, 32: 79-88. PMID: 11604140, DOI: 10.1016/s0896-6273(01)00456-1.Peer-Reviewed Original ResearchConceptsSynaptojanin 1Clathrin-coated intermediatesPolyphosphoinositide phosphatase synaptojanin-1Coat recruitmentActin functionClathrin coatPositive regulatorEndocytic zonesPIPKIgammaSynthesizing enzymesRecruitmentIgammaSynapseDephosphorylationEndocytosisMajor brainElevated levelsRegulatorProteinActinEnzymeMembraneDifferential Expression of Endophilin 1 and 2 Dimers at Central Nervous System Synapses*
Ringstad N, Nemoto Y, De Camilli P. Differential Expression of Endophilin 1 and 2 Dimers at Central Nervous System Synapses*. Journal Of Biological Chemistry 2001, 276: 40424-40430. PMID: 11518713, DOI: 10.1074/jbc.m106338200.Peer-Reviewed Original ResearchConceptsEndophilin-1SH3 domain-mediated interactionsDiverse cellular proteinsDomain-mediated interactionsSynaptic vesicle biogenesisNH2-terminal moietyCoiled-coil domainCentral nervous system synapsesGTPase dynaminVesicle biogenesisDifferent cellular targetsEndocytic machineryCellular proteinsSynaptojanin 1Endophilin isoformsRelated proteinsDifferential expressionCellular targetsStable dimerSynaptojaninDynaminSame complexProteinCentral synapsesFamily members
2000
Amphiphysin 1 Binds the Cyclin-dependent Kinase (cdk) 5 Regulatory Subunit p35 and Is Phosphorylated by cdk5 and cdc2*
Floyd S, Porro E, Slepnev V, Ochoa G, Tsai L, De Camilli P. Amphiphysin 1 Binds the Cyclin-dependent Kinase (cdk) 5 Regulatory Subunit p35 and Is Phosphorylated by cdk5 and cdc2*. Journal Of Biological Chemistry 2000, 276: 8104-8110. PMID: 11113134, DOI: 10.1074/jbc.m008932200.Peer-Reviewed Original ResearchConceptsAmphiphysin 1Kinase familyCyclin-dependent protein kinase familyCyclin-dependent kinase familyProtein kinase familySynaptic vesicle endocytosisB kinase complexNeurite outgrowthSubunit p35Cyclin-dependent kinase 5NH2-terminal regionMitotic phosphorylationYeast homologueImportant physiological roleSerine 272Vesicle endocytosisActin cytoskeletonKinase complexRegulatory subunit p35Actin dynamicsPeripheral lamellipodiaDifferentiated cellsKinase 5AmphiphysinPhysiological roleNobel Celebrates the Neurosciences Modulatory Signaling in the Brain
De Camilli P, Carew T. Nobel Celebrates the Neurosciences Modulatory Signaling in the Brain. Cell 2000, 103: 829-834. PMID: 11136967, DOI: 10.1016/s0092-8674(00)00185-9.Peer-Reviewed Original Research
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
1998
Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
Chen H, Fre S, Slepnev V, Capua M, Takei K, Butler M, Di Fiore P, De Camilli P. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 1998, 394: 793-797. PMID: 9723620, DOI: 10.1038/29555.Peer-Reviewed Original ResearchAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBlotting, NorthernBrainCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCricetinaeEndocytosisMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsProtein BindingRatsRecombinant Fusion ProteinsTransfectionVesicular Transport ProteinsGeneration of Coated Intermediates of Clathrin-Mediated Endocytosis on Protein-Free Liposomes
Takei K, Haucke V, Slepnev V, Farsad K, Salazar M, Chen H, De Camilli P. Generation of Coated Intermediates of Clathrin-Mediated Endocytosis on Protein-Free Liposomes. Cell 1998, 94: 131-141. PMID: 9674434, DOI: 10.1016/s0092-8674(00)81228-3.Peer-Reviewed Original ResearchExpression of Amphiphysin I, an Autoantigen of Paraneoplastic Neurological Syndromes, in Breast Cancer
Floyd S, Butler M, Cremona O, David C, Freyberg Z, Zhang X, Solimena M, Tokunaga A, Ishizu H, Tsutsui K, De Camilli P. Expression of Amphiphysin I, an Autoantigen of Paraneoplastic Neurological Syndromes, in Breast Cancer. Molecular Medicine 1998, 4: 29-39. PMID: 9513187, PMCID: PMC2230265, DOI: 10.1007/bf03401727.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAmino Acid SubstitutionAnimalsAntibodiesAntibodies, MonoclonalAutoantigensAutoimmunityBlotting, WesternBrainBreastBreast NeoplasmsChromatography, AffinityCloning, MolecularFemaleGene ExpressionHumansIsomerismMolecular Sequence DataNerve Tissue ProteinsNervous System DiseasesPolymerase Chain ReactionProtein BiosynthesisRatsStiff-Person SyndromeTumor Cells, CulturedConceptsBreast cancer tissuesBreast cancerCancer tissuesParaneoplastic sensory neuronopathyHuman breast cancer tissuesParaneoplastic neurological syndromesAutoimmune neurological disordersStiff-man syndromeNormal mammary tissueNon-neuronal tissuesAmphiphysin IForms of cancerSensory neuronopathyNeurological syndromeI antibodiesNerve terminalsDominant autoantigenI expressionNeurological disordersMammary tissueCancerAmino acid insertCancer cellsEnhanced expressionKD isoform
1997
The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
Ringstad N, Nemoto Y, De Camilli P. The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 8569-8574. PMID: 9238017, PMCID: PMC23017, DOI: 10.1073/pnas.94.16.8569.Peer-Reviewed Original ResearchConceptsSrc homology 3 domainSynaptic vesicle recyclingDynamin IProtein familyVesicle recyclingSH3 domain-containing proteinsDomain-containing proteinsProline-rich domainTwo-hybrid methodPhysiological binding partnerProline-rich tailRat brain libraryFurther biochemical studiesSH3 domainSynaptojaninDynamin I.Nerve terminal proteinBinding partnerTerminal proteinAmphiphysin IRelated proteinsBrain libraryMultiple tissuesBiochemical studiesProteinThe SH3 Domain of Amphiphysin Binds the Proline-rich Domain of Dynamin at a Single Site That Defines a New SH3 Binding Consensus Sequence*
Grabs D, Slepnev V, Songyang Z, David C, Lynch M, Cantley L, De Camilli P. The SH3 Domain of Amphiphysin Binds the Proline-rich Domain of Dynamin at a Single Site That Defines a New SH3 Binding Consensus Sequence*. Journal Of Biological Chemistry 1997, 272: 13419-13425. PMID: 9148966, DOI: 10.1074/jbc.272.20.13419.Peer-Reviewed Original ResearchConceptsSH3 domainDynamin ILong proline-rich regionProline-rich domainSynaptic vesicle endocytosisProline-rich regionPeptide library approachMultiple SH3Adjacent amino acidsVesicle endocytosisCombinatorial peptide library approachConsensus sequenceAmphiphysinNeuronal proteinsSingle siteAmino acidsSH3Library approachProteinHigh affinityDomainDynaminGTPaseSitesEndocytosisIdentification and characterization of homologues of the Exocyst component Sec10p
Guo W, Roth D, Gatti E, De Camilli P, Novick P. Identification and characterization of homologues of the Exocyst component Sec10p. FEBS Letters 1997, 404: 135-139. PMID: 9119050, DOI: 10.1016/s0014-5793(97)00109-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCloning, MolecularCOS CellsExocytosisFungal ProteinsGolgi ApparatusHumansMammalsMolecular Sequence DataPolymerase Chain ReactionRecombinant ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTranscription, GeneticTransfectionVesicular Transport ProteinsConceptsC. elegans proteinsCharacterization of homologuesAmino acid identityBroad tissue distributionGolgi trafficMammalian counterpartsYeast SaccharomycesAcid identityGene productsCOS cellsWestern blot analysisSec10pPeripheral cytoplasmExocystBlot analysisProteinTissue distributionImmunofluorescence stainingSec8pCellsSaccharomycesCloningHomologuesExocytosisCytoplasm
1996
A presynaptic inositol-5-phosphatase
McPherson P, Garcia E, Slepnev V, David C, Zhang X, Grabs D, Sossini W, Bauerfeind R, Nemoto Y, De Camilli P. A presynaptic inositol-5-phosphatase. Nature 1996, 379: 353-357. PMID: 8552192, DOI: 10.1038/379353a0.Peer-Reviewed Original ResearchConceptsSH3 domainAmino-terminal domainSynaptic vesicle recyclingRelative molecular massPutative functionsNerve terminal proteinSynaptojaninTerminal proteinVesicle recyclingMajor brain proteinsCarboxy terminusTermination sitesMolecular massOculocerebrorenal syndromeSynaptic vesiclesPresynaptic proteinsDynaminPhosphoinositide metabolismProteinBrain proteinsPhospholipid metabolismMetabolismGrb2DomainGenesThe V o Sector of the V-ATPase, Synaptobrevin, and Synaptophysin Are Associated on Synaptic Vesicles in a Triton X-100-resistant, Freeze-thawing Sensitive, Complex (∗)
Galli T, McPherson P, De Camilli P. The V o Sector of the V-ATPase, Synaptobrevin, and Synaptophysin Are Associated on Synaptic Vesicles in a Triton X-100-resistant, Freeze-thawing Sensitive, Complex (∗). Journal Of Biological Chemistry 1996, 271: 2193-2198. PMID: 8567678, DOI: 10.1074/jbc.271.4.2193.Peer-Reviewed Original ResearchMolecular mechanisms in synaptic vesicle recycling
Bauerfeind R, Galli T, De Camilli P. Molecular mechanisms in synaptic vesicle recycling. Brain Cell Biology 1996, 25: 701-715. PMID: 9023719, DOI: 10.1007/bf02284836.Peer-Reviewed Original Research
1995
Targeting of the 67-kDa Isoform of Glutamic Acid Decarboxylase to Intracellular Organelles Is Mediated by Its Interaction with the NH2-terminal Region of the 65-kDa Isoform of Glutamic Acid Decarboxylase (∗)
Dirkx R, Thomas A, Li L, Lernmark Å, Sherwin R, De Camilli P, Solimena M. Targeting of the 67-kDa Isoform of Glutamic Acid Decarboxylase to Intracellular Organelles Is Mediated by Its Interaction with the NH2-terminal Region of the 65-kDa Isoform of Glutamic Acid Decarboxylase (∗). Journal Of Biological Chemistry 1995, 270: 2241-2246. PMID: 7836456, DOI: 10.1074/jbc.270.5.2241.Peer-Reviewed Original ResearchConceptsGolgi complex regionNH2-terminal regionGlutamic acid decarboxylaseAbsence of palmitoylationSoluble cytosolic proteinsAcid decarboxylaseRegions of GAD65Cytosolic proteinsNeurotransmitter gamma-aminobutyric acidDetergent phasePerinuclear regionExtracts of brainIntracellular distributionGamma-aminobutyric acidPellet fractionComplex regionIsoformsProteinFibroblastsGAD67GAD65DecarboxylaseTriton XPalmitoylationNeurons
1993
Autoantibodies to a 128-kd Synaptic Protein in Three Women with the Stiff-Man Syndrome and Breast Cancer
Folli F, Solimena M, Cofiell R, Austoni M, Tallini G, Fasseta G, Bates D, Cartlidge N, Bottazzo G, Piccolo G, De Camilli P. Autoantibodies to a 128-kd Synaptic Protein in Three Women with the Stiff-Man Syndrome and Breast Cancer. New England Journal Of Medicine 1993, 328: 546-551. PMID: 8381208, DOI: 10.1056/nejm199302253280805.Peer-Reviewed Original ResearchMeSH KeywordsAgedAnimalsAutoantibodiesAutoantigensBlotting, WesternBrainBreast NeoplasmsCarcinoma, Intraductal, NoninfiltratingCerebrospinal FluidFemaleGlutamate DecarboxylaseHumansImmunoenzyme TechniquesMiddle AgedNerve Tissue ProteinsParaneoplastic SyndromesPrecipitin TestsRatsStiff-Person SyndromeSynapsesConceptsStiff-man syndromeBreast cancerNervous systemOrgan-specific autoimmune diseasesInsulin-dependent diabetes mellitusSmall invasive ductal carcinomaNervous system antigensPercent of patientsOccult breast cancerSubgroup of patientsInvasive ductal carcinomaDetection of autoantibodiesCentral nervous systemParaneoplastic originControl patientsDiabetes mellitusThird patientDuctal carcinomaAutoimmune diseasesSystem antigensProgressive rigidityAutoantibodiesCerebrospinal fluidRare diseasePatients
1990
Autoantibodies to GABA-ergic Neurons and Pancreatic Beta Cells in Stiff-Man Syndrome
Solimena M, Folli F, Aparisi R, Pozza G, De Camilli P. Autoantibodies to GABA-ergic Neurons and Pancreatic Beta Cells in Stiff-Man Syndrome. New England Journal Of Medicine 1990, 322: 1555-1560. PMID: 2135382, DOI: 10.1056/nejm199005313222202.Peer-Reviewed Original ResearchConceptsStiff-man syndromeInsulin-dependent diabetes mellitusGABA-ergic neuronsGlutamic acid decarboxylaseGamma-aminobutyric acidDiabetes mellitusPancreatic beta cellsAutoimmune diseasesBeta cellsOrgan-specific autoimmune diseasesNeurotransmitter gamma-aminobutyric acidPresence of autoantibodiesGroup of patientsCentral nervous systemPrimary autoantigenUnknown pathogenesisRare disorderAutoantibodiesNervous systemSyndromeUseful markerMellitusAcid decarboxylaseStriking associationPatients