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 vesiclesFission and Uncoating of Synaptic Clathrin-Coated Vesicles Are Perturbed by Disruption of Interactions with the SH3 Domain of Endophilin
Gad H, Ringstad N, Löw P, Kjaerulff O, Gustafsson J, Wenk M, Di Paolo G, Nemoto Y, Crum J, Ellisman M, De Camilli P, Shupliakov O, Brodin L. Fission and Uncoating of Synaptic Clathrin-Coated Vesicles Are Perturbed by Disruption of Interactions with the SH3 Domain of Endophilin. Neuron 2000, 27: 301-312. PMID: 10985350, DOI: 10.1016/s0896-6273(00)00038-6.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBinding, CompetitiveCarrier ProteinsClathrinCloning, MolecularCoated Pits, Cell-MembraneDynaminsGTP PhosphohydrolasesLampreysMicroinjectionsMolecular Sequence DataNerve Tissue ProteinsPeptide FragmentsPhosphoric Monoester HydrolasesSequence Homology, Amino AcidSrc Homology DomainsSynaptic VesiclesConceptsProline-rich domainSynaptic vesicle endocytosisSH3 domainVesicle endocytosisEndophilin's SH3 domainClathrin coat formationClathrin-coated vesiclesClathrin-coated pitsDisruption of interactionsEndocytic intermediatesProteinprotein interactionsCoat formationEndophilinMolecular switchUncoatingEndocytosisVesiclesTandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*
Slepnev V, Ochoa G, Butler M, De Camilli P. Tandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*. Journal Of Biological Chemistry 2000, 275: 17583-17589. PMID: 10748223, DOI: 10.1074/jbc.m910430199.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesBinding, CompetitiveCHO CellsClathrinCricetinaeGlutathione TransferaseHumansMembrane ProteinsMolecular Sequence DataMonomeric Clathrin Assembly ProteinsMutagenesis, Site-DirectedNerve Tissue ProteinsPeptide FragmentsRecombinant Fusion ProteinsTransfectionConceptsAP-2Amphiphysin 1Coat proteinClathrin adaptor AP-2COOH-terminal SH3 domainAdaptor AP-2Chinese hamster ovary cellsCoat functionMultifunctional adaptorSH3 domainHamster ovary cellsTerminal domainBinding domainsClathrinDynaminMembrane lipidsAmphiphysinSynaptic vesiclesAmino acidsSynaptojaninOvary cellsDirect interactionProteinTertiary complexTandem arrangement
1998
Perturbation of Dynamin II with an Amphiphysin SH3 Domain Increases GLUT4 Glucose Transporters at the Plasma Membrane in 3T3-L1 Adipocytes DYNAMIN II PARTICIPATES IN GLUT4 ENDOCYTOSIS*
Volchuk A, Narine S, Foster L, Grabs D, De Camilli P, Klip A. Perturbation of Dynamin II with an Amphiphysin SH3 Domain Increases GLUT4 Glucose Transporters at the Plasma Membrane in 3T3-L1 Adipocytes DYNAMIN II PARTICIPATES IN GLUT4 ENDOCYTOSIS*. Journal Of Biological Chemistry 1998, 273: 8169-8176. PMID: 9525921, DOI: 10.1074/jbc.273.14.8169.Peer-Reviewed Original ResearchConceptsGLUT4 endocytosisDynamin IIGLUT4 glucose transportersPlasma membraneCell surfaceSH3 domainClathrin-coated vesicle formationFusion proteinGlucose transporterLevels of GLUT4Amphiphysin SH3 domainLow-density microsomal fractionIsolated plasma membranesTransferrin endocytosisEndocytic systemGLUT4 internalizationProtein dynaminGlutathione S-transferaseEndosomal compartmentsGLUT4 distributionVesicle formationDynamin peptideEndocytosisGLUT4S-transferase
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 affinityDomainDynaminGTPaseSitesEndocytosisSynaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions
Shupliakov O, Löw P, Grabs D, Gad H, Chen H, David C, Takei K, De Camilli P, Brodin L. Synaptic Vesicle Endocytosis Impaired by Disruption of Dynamin-SH3 Domain Interactions. Science 1997, 276: 259-263. PMID: 9092476, DOI: 10.1126/science.276.5310.259.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell MembraneCoated Pits, Cell-MembraneDynaminsEndocytosisGTP PhosphohydrolasesHumansLampreysMicroscopy, ElectronMolecular Sequence DataNerve Tissue ProteinsProlineRecombinant Fusion ProteinsSrc Homology DomainsSynapsesSynaptic TransmissionSynaptic VesiclesConceptsSynaptic vesicle endocytosisSH3 domainVesicle endocytosisSrc homology 3 (SH3) domain-containing proteinsDomain-containing proteinsClathrin-coated pitsClathrin-mediated endocytosisSH3 binding siteAmphiphysin SH3 domainSynaptic vesicle recyclingCOOH-terminal regionDynamin bindsDynamin functionBinding partnerVesicle recyclingDomain interactionsDynamin peptidePhysiological roleEndocytosisEssential roleBinding sitesSynaptic architectureSH3DomainAmphiphysin
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 metabolismMetabolismGrb2DomainGenes
1994
Autoimmunity in Stiff‐Man Syndrome with breast cancer is targeted to the C‐terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161
David C, Solimena M, De Camilli P. Autoimmunity in Stiff‐Man Syndrome with breast cancer is targeted to the C‐terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161. FEBS Letters 1994, 351: 73-79. PMID: 8076697, DOI: 10.1016/0014-5793(94)00826-4.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAutoantibodiesBase SequenceBreast NeoplasmsChickensCloning, MolecularCytoskeletal ProteinsFungal ProteinsHumansMicrofilament ProteinsMolecular Sequence DataNerve Tissue ProteinsOligodeoxyribonucleotidesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidStiff-Person SyndromeConceptsC-terminal regionStiff-man syndromeYeast proteinsUnfavourable growth conditionsBreast cancerSH3 domainTerminal domainAmphiphysinNeuronal proteinsRvs167Rvs161ProteinCell entryPatient autoantibodiesGrowth conditionsSynaptic membranesSyndromeCancerDistinct patternsStationary phaseDomainChickensAutoantibodiesAutoimmunityAutoantigens