2000
Specificity of the Binding of Synapsin I to Src Homology 3 Domains*
Onofri F, Giovedı̀ S, Kao H, Valtorta F, Borbone L, De Camilli P, Greengard P, Benfenati F. Specificity of the Binding of Synapsin I to Src Homology 3 Domains*. Journal Of Biological Chemistry 2000, 275: 29857-29867. PMID: 10899172, DOI: 10.1074/jbc.m006018200.Peer-Reviewed Original ResearchConceptsSrc homology 3 domainSH3 domainCOOH-terminal regionSynapsin ISignal transductionC-SrcSynaptic vesicle-associated phosphoproteinsMultiple SH3 domainsGTPase-activating proteinsProtein-protein interactionsMitogen-activated protein kinaseDependent protein kinase IIProtein kinase IICytoskeleton assemblyP85 subunitDistinct binding patternsHigh-affinity interactionProtein kinaseAmphiphysin IC gammaKinase IIAlpha-spectrinGrb2SH3Synaptic vesicles
1999
Amphiphysin and Breast Cancer
DeCamilli P. Amphiphysin and Breast Cancer. 1999 DOI: 10.21236/ada383728.Peer-Reviewed Original ResearchBreast cancerWestern blottingStiff-man syndromeBreast cancer patientsBreast cancer cell linesLarge case loadsNon-neuronal tissuesOccult neoplasiaCancer cell linesCancer patientsNerve terminal proteinLow-level expressionBreast tumorsNeurological diseasesAutoantibodiesPatientsCancerAmphiphysin ICase loadRT-PCREnhanced expressionCell linesIntracellular signalingBlottingCyclin-dependent kinase gene family
1998
Amphiphysin I Antisense Oligonucleotides Inhibit Neurite Outgrowth in Cultured Hippocampal Neurons
Mundigl O, Ochoa G, David C, Slepnev V, Kabanov A, De Camilli P. Amphiphysin I Antisense Oligonucleotides Inhibit Neurite Outgrowth in Cultured Hippocampal Neurons. Journal Of Neuroscience 1998, 18: 93-103. PMID: 9412489, PMCID: PMC6793426, DOI: 10.1523/jneurosci.18-01-00093.1998.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCalcium-Binding ProteinsCells, CulturedDynamin IDynaminsEndocytosisGene ExpressionGTP PhosphohydrolasesHippocampusMembrane GlycoproteinsMiceNerve Tissue ProteinsNeuritesOligonucleotides, AntisensePhosphoric Monoester HydrolasesRabbitsRatsRNA, MessengerSynaptic VesiclesSynaptotagminsTubulinConceptsAmphiphysin IDynamin ICell polarityNeurite outgrowthSynaptic vesicle endocytosisPhysiological binding partnerGrowth conesClose functional linkYeast homologActin patchesActin functionVesicle endocytosisActin dynamicsProtein familyBinding partnerCell cytoskeletonAxon formationFunctional linkNeuronal differentiationWestern blot analysisCultured hippocampal neuronsHippocampal neuronsDevelopmental stagesNeuronal proteinsAmphipathic polymersExpression 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
Amphiphysin I Is Associated with Coated Endocytic Intermediates and Undergoes Stimulation-dependent Dephosphorylation in Nerve Terminals*
Bauerfeind R, Takei K, De Camilli P. Amphiphysin I Is Associated with Coated Endocytic Intermediates and Undergoes Stimulation-dependent Dephosphorylation in Nerve Terminals*. Journal Of Biological Chemistry 1997, 272: 30984-30992. PMID: 9388246, DOI: 10.1074/jbc.272.49.30984.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcineurinDynamin IDynaminsElectrophoresis, Polyacrylamide GelEndocytosisEnzyme InhibitorsGTP PhosphohydrolasesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Microscopy, ElectronMicrotubulesNerve Tissue ProteinsPhospholipase DPhosphoric Monoester HydrolasesPhosphorylationPresynaptic TerminalsRatsConceptsSrc homology 3Dynamin IAmphiphysin IEndocytic intermediatesCalcineurin-dependent dephosphorylationSynaptic vesicle endocytosisSynaptic vesicle exocytosisSynaptic vesicle recyclingClathrin-coated budsBurst of exocytosisAbundant presynaptic proteinElectron microscopy immunocytochemistryHomology 3Vesicle endocytosisVesicle exocytosisConstitutive phosphorylationVesicle recyclingRapid dephosphorylationOkadaic acidPhysiological partnersDephosphorylationBinding proteinPutative rolePresynaptic proteinsProteinThe 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 studiesProtein