2023
RBG Motif Bridge-Like Lipid Transport Proteins: Structure, Functions, and Open Questions
Hanna M, Guillén-Samander A, De Camilli P. RBG Motif Bridge-Like Lipid Transport Proteins: Structure, Functions, and Open Questions. Annual Review Of Cell And Developmental Biology 2023, 39: 409-434. PMID: 37406299, DOI: 10.1146/annurev-cellbio-120420-014634.Peer-Reviewed Original ResearchLipid transfer proteinMembrane contact sitesVesicle-mediated trafficTransport of lipidsPutative physiological roleEukaryotic cellsEndocytic pathwayContact sitesLipid transportPhysiological roleTransfer proteinProteinHydrophobic channelRod-like structureLipidsEntire lengthDevelopmental disordersCytosolMutationsNew familyTransportPathwayMechanismMembraneCells
2000
Amphiphysin 1 Binds the Cyclin-dependent Kinase (cdk) 5 Regulatory Subunit p35 and Is Phosphorylated by cdk5 and cdc2*
Floyd S, Porro E, Slepnev V, Ochoa G, Tsai L, De Camilli P. Amphiphysin 1 Binds the Cyclin-dependent Kinase (cdk) 5 Regulatory Subunit p35 and Is Phosphorylated by cdk5 and cdc2*. Journal Of Biological Chemistry 2000, 276: 8104-8110. PMID: 11113134, DOI: 10.1074/jbc.m008932200.Peer-Reviewed Original ResearchConceptsAmphiphysin 1Kinase familyCyclin-dependent protein kinase familyCyclin-dependent kinase familyProtein kinase familySynaptic vesicle endocytosisB kinase complexNeurite outgrowthSubunit p35Cyclin-dependent kinase 5NH2-terminal regionMitotic phosphorylationYeast homologueImportant physiological roleSerine 272Vesicle endocytosisActin cytoskeletonKinase complexRegulatory subunit p35Actin dynamicsPeripheral lamellipodiaDifferentiated cellsKinase 5AmphiphysinPhysiological roleDual interaction of synaptotagmin with μ2‐ and α‐adaptin facilitates clathrin‐coated pit nucleation
Haucke V, Wenk M, Chapman E, Farsad K, De Camilli P. Dual interaction of synaptotagmin with μ2‐ and α‐adaptin facilitates clathrin‐coated pit nucleation. The EMBO Journal 2000, 19: 6011-6019. PMID: 11080148, PMCID: PMC305843, DOI: 10.1093/emboj/19.22.6011.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 1Adaptor Protein Complex 2Adaptor Protein Complex 3Adaptor Protein Complex alpha SubunitsAdaptor Protein Complex mu SubunitsAdaptor Proteins, Vesicular TransportAnimalsBinding SitesCalcium-Binding ProteinsCHO CellsClathrinCoated Pits, Cell-MembraneCricetinaeIn Vitro TechniquesLiposomesLysineMembrane GlycoproteinsMembrane ProteinsMutationNerve Tissue ProteinsPhosphoproteinsProtein SubunitsRatsSynaptic VesiclesSynaptotagminsTyrosineConceptsAP-2C2B domainEndocytic adaptor complex AP-2Endocytic clathrin-coated pitsAdaptor complex AP-2Clathrin adaptor AP-2Synaptic vesicle protein synaptotagminTyrosine-based sorting motifAdaptor AP-2Clathrin-coated pitsMajor docking siteKey physiological rolesDual interactionSorting motifClathrin coatTransferrin internalizationProtein synaptotagminDocking siteSubdomain BSynaptotagminPhysiological roleLiving cellsSynaptic vesiclesSubunitsMu2
1997
Synaptic 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
1990
Substance P-like immunoreactivity at the frog neuromuscular junction
Matteoli M, Haimann C, De Camilli P. Substance P-like immunoreactivity at the frog neuromuscular junction. Neuroscience 1990, 37: 271-275. PMID: 1700842, DOI: 10.1016/0306-4522(90)90213-n.Peer-Reviewed Original ResearchConceptsLike immunoreactivitySubstance PNerve terminalsCalcitonin gene-related peptide-like immunoreactivityGene-related peptide-like immunoreactivityFrog motor nerve endingsPeptide-like immunoreactivityMotor nerve endingsLarge dense-core vesiclesFrog neuromuscular junctionDense-core vesiclesCholinergic transmissionNerve endingsSame neuronsNeuromuscular junctionImmunoreactivityFrog motoneuronsPhysiological roleImmunofluorescence approachPrevious dataMotoneuronsNeurons