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 disordersParkinsonism Sac domain mutation in Synaptojanin-1 affects ciliary properties in iPSC-derived dopaminergic neurons
Rafiq N, Fujise K, Rosenfeld M, Xu P, De Camilli P. Parkinsonism Sac domain mutation in Synaptojanin-1 affects ciliary properties in iPSC-derived dopaminergic neurons. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2318943121. PMID: 38635628, PMCID: PMC11047088, DOI: 10.1073/pnas.2318943121.Peer-Reviewed Original ResearchConceptsSynaptojanin 1Endocytic factorsDA neuronsCilia-mediated signalingNerve terminalsIPSC-derived dopaminergic neuronsUbiquitin chainsUbiquitinated proteinsCiliary baseCilia lengthNeurological defectsDopaminergic neuronsProtein dynamicsDomain mutationsAssembly stateIsogenic controlsNeuronsAbnormal accumulationMutationsMiceFocal concentrationParkinsonPI(4UbiquitinEndocytosis
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
2020
Role of VPS13, a protein with similarity to ATG2, in physiology and disease
Ugur B, Hancock-Cerutti W, Leonzino M, De Camilli P. Role of VPS13, a protein with similarity to ATG2, in physiology and disease. Current Opinion In Genetics & Development 2020, 65: 61-68. PMID: 32563856, PMCID: PMC7746581, DOI: 10.1016/j.gde.2020.05.027.Peer-Reviewed Original ResearchConceptsAutophagy protein ATG2N-terminal halfVPS13 proteinsMolecular functionsCellular processesFamily proteinsVps13Contact sitesAtg2Intracellular organellesFunctional studiesNovel mechanismProteinSimilar roleHydrophobic channelStructural studiesNeurodegenerative disordersPhysiologyDirect transferOrganellesSimilarityMutationsRoleLipidsBilayersAbsence 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
2017
Parkinson Sac Domain Mutation in Synaptojanin 1 Impairs Clathrin Uncoating at Synapses and Triggers Dystrophic Changes in Dopaminergic Axons
Cao M, Wu Y, Ashrafi G, McCartney AJ, Wheeler H, Bushong EA, Boassa D, Ellisman MH, Ryan TA, De Camilli P. Parkinson Sac Domain Mutation in Synaptojanin 1 Impairs Clathrin Uncoating at Synapses and Triggers Dystrophic Changes in Dopaminergic Axons. Neuron 2017, 93: 882-896.e5. PMID: 28231468, PMCID: PMC5340420, DOI: 10.1016/j.neuron.2017.01.019.Peer-Reviewed Original ResearchConceptsDopaminergic axonsEarly-onset parkinsonism patientsEndocytic dysfunctionNeurological manifestationsParkinsonism patientsDystrophic changesParkinson's diseaseDorsal striatumHuman patientsClathrin-coated intermediatesParkin levelsHomozygous mutationMutant brainsSynaptojanin 1Domain mutationsTerminal changesPatientsStriking accumulationAxonsDiseaseMiceSynapsesSynaptic vesicle endocytosisMutationsDysfunction
1998
Endocytosis proteins and cancer: a potential link?
Floyd S, De Camilli P. Endocytosis proteins and cancer: a potential link? Trends In Cell Biology 1998, 8: 299-301. PMID: 9704404, DOI: 10.1016/s0962-8924(98)01316-6.Peer-Reviewed Original ResearchConceptsEndocytosis proteinsVariety of proteinsHuman haematopoietic malignanciesReceptor-mediated endocytosisAbnormal expressionClathrin adaptorsBiology of cancerChromosomal rearrangementsHuman cancersProteinHaematopoietic malignanciesRecent studiesPotential mechanismsExpressionPotential linkClathrinEndocytosisGenesAdaptorBiologyMutationsRearrangementCancerTarget