2020
Absence of Sac2/INPP5F enhances the phenotype of a Parkinson’s disease mutation of synaptojanin 1
Cao M, Park D, Wu Y, De Camilli P. Absence of Sac2/INPP5F enhances the phenotype of a Parkinson’s disease mutation of synaptojanin 1. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 12428-12434. PMID: 32424101, PMCID: PMC7275725, DOI: 10.1073/pnas.2004335117.Peer-Reviewed Original ResearchConceptsSynaptojanin 1Sac domain-containing proteinsDisease mutationsDomain-containing proteinsGenome-wide association studiesPD risk lociSynaptic vesicle recyclingEndocytic factorsPD risk genesPhosphatase domainPhosphoinositide phosphataseParkinson's diseaseNumerous genesParkinson’s disease mutationsVesicle recyclingRisk lociAssociation studiesRisk genesInactivating mutationStriatal dopaminergic nerve terminalsGenesOccasional survivorsMutationsDopaminergic nerve terminalsSJ1
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 studiesProteinSynaptic 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