2023
ATG9 vesicles comprise the seed membrane of mammalian autophagosomes
Olivas T, Wu Y, Yu S, Luan L, Choi P, Guinn E, Nag S, De Camilli P, Gupta K, Melia T. ATG9 vesicles comprise the seed membrane of mammalian autophagosomes. Journal Of Cell Biology 2023, 222: e202208088. PMID: 37115958, PMCID: PMC10148236, DOI: 10.1083/jcb.202208088.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutophagosomesAutophagyAutophagy-Related ProteinsLipidsMammalsMembrane ProteinsProtein TransportConceptsAtg9 vesiclesMammalian autophagosomesStyrene maleic acid lipid particlesLipid scramblase activityLC3-IIAutophagosomes formAutophagosome membraneMature autophagosomesScramblase activityAutophagosome formationAtg9Lipid transportMembrane growthAutophagosomesNanoscale organizationProtein-mediated transferProteinMembrane surface areaOrganellesVesiclesSeed membraneMembraneLipid particlesLipidsDifferent stages
2022
Presynaptic autophagy is coupled to the synaptic vesicle cycle via ATG-9
Yang S, Park D, Manning L, Hill SE, Cao M, Xuan Z, Gonzalez I, Dong Y, Clark B, Shao L, Okeke I, Almoril-Porras A, Bai J, De Camilli P, Colón-Ramos DA. Presynaptic autophagy is coupled to the synaptic vesicle cycle via ATG-9. Neuron 2022, 110: 824-840.e10. PMID: 35065714, PMCID: PMC9017068, DOI: 10.1016/j.neuron.2021.12.031.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutophagyAutophagy-Related ProteinsCaenorhabditis elegansEndocytosisPresynaptic TerminalsSynaptic VesiclesConceptsSynaptic vesicle cycleVesicle cyclePresynaptic autophagyAutophagosome biogenesisATG-9Only transmembrane proteinTrans-Golgi networkCellular degradation pathwayPresynaptic sitesActivity-dependent mannerTransmembrane proteinSynaptojanin 1Synaptic fociBiogenesisAutophagyNeuronal healthDegradation pathwayTraffickingPathwayParkinson's diseaseSynaptic activityNeuronal activityElegansSitesEndocytosis
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
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 ResearchMeSH KeywordsAutophagy-Related ProteinsBrainHumansNeurodegenerative DiseasesNeurodevelopmental DisordersVesicular Transport ProteinsConceptsAutophagy protein ATG2N-terminal halfVPS13 proteinsMolecular functionsCellular processesFamily proteinsVps13Contact sitesAtg2Intracellular organellesFunctional studiesNovel mechanismProteinSimilar roleHydrophobic channelStructural studiesNeurodegenerative disordersPhysiologyDirect transferOrganellesSimilarityMutationsRoleLipidsBilayers
2018
VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites
Kumar N, Leonzino M, Hancock-Cerutti W, Horenkamp FA, Li P, Lees JA, Wheeler H, Reinisch KM, De Camilli P. VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites. Journal Of Cell Biology 2018, 217: 3625-3639. PMID: 30093493, PMCID: PMC6168267, DOI: 10.1083/jcb.201807019.Peer-Reviewed Original ResearchConceptsN-terminal portionAutophagy protein ATG2Membrane lipid homeostasisLate endosomes/lysosomesSecondary structure similarityLipid transport proteinsER contact sitesEndosomes/lysosomesHuman VPS13AVPS13 genesVps13Implicating defectsTransport proteinsLipid transportersContact sitesGenetic studiesLipid homeostasisLipid exchangeTransport roleProteinOrganellesVPS13ANeurodegenerative disordersStructure similarityHydrophobic cavity