2024
VPS13B is localized at the interface between Golgi cisternae and is a functional partner of FAM177A1
Ugur B, Schueder F, Shin J, Hanna M, Wu Y, Leonzino M, Su M, McAdow A, Wilson C, Postlethwait J, Solnica-Krezel L, Bewersdorf J, De Camilli P. VPS13B is localized at the interface between Golgi cisternae and is a functional partner of FAM177A1. Journal Of Cell Biology 2024, 223: e202311189. PMID: 39331042, PMCID: PMC11451052, DOI: 10.1083/jcb.202311189.Peer-Reviewed Original ResearchConceptsLipid transportGolgi complex proteinGolgi subcompartmentsGolgi membranesGolgi cisternaeProtein familyFunctional partnersGolgi complexKO cellsComplex proteinsFAM177A1GolgiVPS13BAdjacent membranesMutationsProteinCohen syndromeLipidOrthologsInteractorsBrefeldinMembraneOrganellesSubcompartmentsDevelopmental disorders
2021
Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport
Leonzino M, Reinisch KM, De Camilli P. Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport. Biochimica Et Biophysica Acta (BBA) - Molecular And Cell Biology Of Lipids 2021, 1866: 159003. PMID: 34216812, PMCID: PMC8325632, DOI: 10.1016/j.bbalip.2021.159003.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutophagosomesAutophagy-Related ProteinsCryoelectron MicroscopyDisease Models, AnimalEukaryotic CellsHeredodegenerative Disorders, Nervous SystemHumansHydrophobic and Hydrophilic InteractionsLipid BilayersLipid MetabolismMitochondrial MembranesMutationProtein DomainsStructure-Activity RelationshipVesicular Transport ProteinsYeastsConceptsLipid transportMembrane contact sitesDomain protein familyOccurrence of proteinsVPS13 proteinsEukaryotic cellsNumerous proteinsProtein familyIntracellular membranesProtein bridgeHydrophobic grooveContact sitesMembrane growthLipid transferBilayer lipidsNovel mechanismVps13New mechanismProteinLipidsAtg2OrganellesAdjacent bilayersDiscoveryMechanism
1999
The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*
Rosenthal J, Chen H, Slepnev V, Pellegrini L, Salcini A, Di Fiore P, De Camilli P. The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*. Journal Of Biological Chemistry 1999, 274: 33959-33965. PMID: 10567358, DOI: 10.1074/jbc.274.48.33959.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCoated VesiclesCricetinaeDNA, ComplementaryFluorescent Antibody TechniqueGene ExpressionHumansIntracellular Signaling Peptides and ProteinsLuciferasesMaleMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsPhylogenyProtein BindingProtein Structure, TertiaryRatsRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue DistributionVesicular Transport ProteinsConceptsEpsin 1Clathrin coatClathrin adaptor AP-2New protein modulesNew protein familyTerminal regionAdaptor AP-2Family of proteinsRat brain libraryNPF motifsProtein modulesProtein familyCell peripheryAP-2Membrane dynamicsSimilar proteinsBrain libraryClathrinEps15Vesicle fractionEpsinGreen fluorescentGolgi regionCell surfaceProtein
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
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 studiesProtein