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 levelsRegulatorProteinActinEnzymeMembrane
2000
Synaptic Autoimmunity and the Salk Factor
Solimena M, De Camilli P. Synaptic Autoimmunity and the Salk Factor. Neuron 2000, 28: 309-316. PMID: 11144336, DOI: 10.1016/s0896-6273(00)00105-7.Peer-Reviewed Original ResearchSpecificity 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
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 polymers
1997
Amphiphysin II (SH3P9; BIN1), a Member of the Amphiphysin/Rvs Family, Is Concentrated in the Cortical Cytomatrix of Axon Initial Segments and Nodes of Ranvier in Brain and around T Tubules in Skeletal Muscle
Butler M, David C, Ochoa G, Freyberg Z, Daniell L, Grabs D, Cremona O, De Camilli P. Amphiphysin II (SH3P9; BIN1), a Member of the Amphiphysin/Rvs Family, Is Concentrated in the Cortical Cytomatrix of Axon Initial Segments and Nodes of Ranvier in Brain and around T Tubules in Skeletal Muscle. Journal Of Cell Biology 1997, 137: 1355-1367. PMID: 9182667, PMCID: PMC2132527, DOI: 10.1083/jcb.137.6.1355.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsAxonsBase SequenceBrain ChemistryCarrier ProteinsCerebral CortexCloning, MolecularCOS CellsCytoplasmDNA, ComplementaryGene ExpressionHumansMiceMolecular Sequence DataMuscle ProteinsMuscle, SkeletalNerve Tissue ProteinsNuclear ProteinsRabbitsRanvier's NodesRatsSrc Homology DomainsTumor Cells, CulturedTumor Suppressor ProteinsConceptsAmphiphysin IICortical cytoplasmPresence of clathrinSkeletal muscleParaneoplastic stiff-man syndromeAxon initial segmentYeast homologueActin functionNuclear functionsActin cytoskeletonActin dynamicsMammalian cellsActin cytomatrixPleiotropic functionsDistinct domainsNeuronal proteinsSplice variantsT-tubulesAmphiphysinCytomatrixEndocytosisPutative roleNodes of RanvierCytoplasmIsoformsThe 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 affinityDomainDynaminGTPaseSitesEndocytosis