2000
Fission 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 switchUncoatingEndocytosisVesicles
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 affinityDomainDynaminGTPaseSitesEndocytosis