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
2022
A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane
Guillén-Samander A, Wu Y, Pineda SS, García FJ, Eisen JN, Leonzino M, Ugur B, Kellis M, Heiman M, De Camilli P. A partnership between the lipid scramblase XK and the lipid transfer protein VPS13A at the plasma membrane. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2205425119. PMID: 35994651, PMCID: PMC9436381, DOI: 10.1073/pnas.2205425119.Peer-Reviewed Original ResearchConceptsCaudate neuronsClinical manifestationsExposure of PtdSerPH domainMcLeod syndromeCell surface exposureER-PM contactsLipid dropletsTransport of lipidsPutative roleUnknown mechanismNeuronsLipid transfer proteinVPS13ALipid scramblasesTransfer proteinCytosolic loopExposurePlasma membraneCell surfaceEndoplasmic reticulumLipid transferERSyndromeDisease
2020
BICRA, a SWI/SNF Complex Member, Is Associated with BAF-Disorder Related Phenotypes in Humans and Model Organisms
Barish S, Barakat T, Michel B, Mashtalir N, Phillips J, Valencia A, Ugur B, Wegner J, Scott T, Bostwick B, Network U, Murdock D, Dai H, Perenthaler E, Nikoncuk A, van Slegtenhorst M, Brooks A, Keren B, Nava C, Mignot C, Douglas J, Rodan L, Nowak C, Ellard S, Stals K, Lynch S, Faoucher M, Lesca G, Edery P, Engleman K, Zhou D, Thiffault I, Herriges J, Gass J, Louie R, Stolerman E, Washington C, Vetrini F, Otsubo A, Pratt V, Conboy E, Treat K, Shannon N, Camacho J, Wakeling E, Yuan B, Chen C, Rosenfeld J, Westerfield M, Wangler M, Yamamoto S, Kadoch C, Scott D, Bellen H. BICRA, a SWI/SNF Complex Member, Is Associated with BAF-Disorder Related Phenotypes in Humans and Model Organisms. American Journal Of Human Genetics 2020, 107: 1096-1112. PMID: 33232675, PMCID: PMC7820627, DOI: 10.1016/j.ajhg.2020.11.003.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAnimalsChildChild, PreschoolChromosomal Proteins, Non-HistoneDevelopmental DisabilitiesDrosophila melanogasterDrosophila ProteinsFemaleGenes, DominantGenetic VariationHaploinsufficiencyHumansInfantMaleMicroscopy, ConfocalMutation, MissenseNeurogliaNeuronsPhenotypeProtein BindingTumor Suppressor ProteinsZebrafishZebrafish ProteinsConceptsSWI/SNF complex membersComplex membersSWI/SNF familyPosition-effect variegationIntellectual disability disordersContext-specific mannerNcBAF complexesDrosophila orthologDominant enhancersBAF complexModel organismsFunctional characterizationDisability disordersCraniofacial defectsNeurodevelopmental phenotypesOrthologsRelated phenotypesPhenotypeFunction variantsRare neurodevelopmental disorderGenesRare variantsFliesPathogenic variantsNeurodevelopmental disordersRole 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 transferOrganellesSimilarityMutationsRoleLipidsBilayers
2019
cindr, the Drosophila Homolog of the CD2AP Alzheimer’s Disease Risk Gene, Is Required for Synaptic Transmission and Proteostasis
Ojelade S, Lee T, Giagtzoglou N, Yu L, Ugur B, Li Y, Duraine L, Zuo Z, Petyuk V, De Jager P, Bennett D, Arenkiel B, Bellen H, Shulman J. cindr, the Drosophila Homolog of the CD2AP Alzheimer’s Disease Risk Gene, Is Required for Synaptic Transmission and Proteostasis. Cell Reports 2019, 28: 1799-1813.e5. PMID: 31412248, PMCID: PMC6703184, DOI: 10.1016/j.celrep.2019.07.041.Peer-Reviewed Original ResearchConceptsPlasma membrane calcium ATPaseDisease risk genesDisease susceptibility genesSynaptic vesicle recyclingUbiquitin-proteasome systemMembrane calcium ATPaseAlzheimer’s disease risk genesDrosophila homologConserved roleAlzheimer's disease susceptibility genesSynaptic proteostasisAdaptor proteinNeuronal requirementsVesicle recyclingProteostasisCindrRisk genesSusceptibility genesSynapse maturationHuman postmortem brainHuman tauProtein levelsNeurofibrillary tangle pathologyNull miceAD susceptibility
2016
Drosophila tools and assays for the study of human diseases
Ugur B, Chen K, Bellen HJ. Drosophila tools and assays for the study of human diseases. Disease Models & Mechanisms 2016, 9: 235-244. PMID: 26935102, PMCID: PMC4833332, DOI: 10.1242/dmm.023762.Peer-Reviewed Original ResearchConceptsHuman diseasesHuman disease-causing genesUse of DrosophilaDrosophila melanogasterDisease-causing genesMolecular parallelsSpecific genesMolecular mechanismsPhysiological processesPathogenic mechanismsMorphological differencesCellular featuresFliesGenesMolecular pathogenesisInternal organ systemsAssaysCentral nervous systemDrosophilaMelanogasterVertebratesPowerful toolNervous systemOrgan systemsOrganisms