2022
Proximity proteomics of synaptopodin provides insight into the molecular composition of the spine apparatus of dendritic spines
Falahati H, Wu Y, Feuerer V, Simon HG, De Camilli P. Proximity proteomics of synaptopodin provides insight into the molecular composition of the spine apparatus of dendritic spines. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2203750119. PMID: 36215465, PMCID: PMC9586327, DOI: 10.1073/pnas.2203750119.Peer-Reviewed Original ResearchConceptsSpine apparatusDendritic spinesSubset of neuronsAxon initial segmentDendritic shaftsER cisternsNonneuronal cellsSynaptopodinSpineSmooth endoplasmic reticulumEndoplasmic reticulumCisternal organelleInitial segmentSpecific localizationCisternsBinding proteinPDLIM7Expression patternsSubsetProteinSmall subsetDiseaseNeuronsBrainFunctional partnership
1999
Epidermal growth factor pathway substrate 15, Eps15
Salcini A, Chen H, Iannolo G, De Camilli P, Di Fiore P. Epidermal growth factor pathway substrate 15, Eps15. The International Journal Of Biochemistry & Cell Biology 1999, 31: 805-809. PMID: 10481267, DOI: 10.1016/s1357-2725(99)00042-4.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsCalcium-Binding ProteinsCarrier ProteinsCell LineChromosomes, Human, Pair 1EndocytosisEpidermal Growth FactorHumansIntracellular Signaling Peptides and ProteinsNeuropeptidesPhosphoproteinsSignal TransductionTransferrinVesicular Transport ProteinsConceptsEpidermal growth factor receptorPutative coiled-coil regionCoiled-coil regionCell proliferationNIH 3T3 cellsReceptor-mediated endocytosisEH domainNH2-terminal portionEndocytic machineryEpsin functionIntracellular sortingEps15Growth factor receptorTerminal domainAP-2Kinase activityBinding proteinMultiple copiesBiomolecular strategiesProteinFactor receptorTripartite structureMLL geneGenesProliferation
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 proteinsProteinSynapsin I interacts with c-Src and stimulates its tyrosine kinase activity
Onofri F, Giovedì S, Vaccaro P, Czernik A, Valtorta F, De Camilli P, Greengard P, Benfenati F. Synapsin I interacts with c-Src and stimulates its tyrosine kinase activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 12168-12173. PMID: 9342381, PMCID: PMC23739, DOI: 10.1073/pnas.94.22.12168.Peer-Reviewed Original ResearchConceptsTyrosine kinase activityC-SrcKinase activitySynapsin ISrc homology 3 domainNonreceptor tyrosine kinase c-SrcSynaptic vesicle-associated phosphoproteinsTyrosine kinase c-SrcSynaptic vesiclesC-Src SH3 domainKinase c-SrcEndogenous tyrosine kinase activityTotal cellular poolStoichiometric phosphorylationSynaptic vesicle preparationsCoprecipitation assaysSignal transductionProtein speciesCellular poolRegulatory sitesBinding proteinVesicle preparationsDetergent extractsSeveralfold stimulationAffinity chromatography
1986
Interaction of the Regulatory Subunit (RII) of cAMP‐Dependent Protein Kinase with Tissue‐Specific Binding Proteins Including Microtubule‐Associated Proteinsa
LOHMANN S, WALTER U, DeCAMILLI P. Interaction of the Regulatory Subunit (RII) of cAMP‐Dependent Protein Kinase with Tissue‐Specific Binding Proteins Including Microtubule‐Associated Proteinsa. Annals Of The New York Academy Of Sciences 1986, 466: 449-452. PMID: 3460424, DOI: 10.1111/j.1749-6632.1986.tb38421.x.Peer-Reviewed Original Research