2021
VPS13D bridges the ER to mitochondria and peroxisomes via Miro
Guillén-Samander A, Leonzino M, Hanna MG, Tang N, Shen H, De Camilli P. VPS13D bridges the ER to mitochondria and peroxisomes via Miro. Journal Of Cell Biology 2021, 220: e202010004. PMID: 33891013, PMCID: PMC8077184, DOI: 10.1083/jcb.202010004.Peer-Reviewed Original ResearchConceptsLipid transport proteinsHigher eukaryotesER-mitochondriaSecretory pathwayAccessory factorsMitochondrial dynamicsDisease pathogenesisTransport proteinsParkin substratesLipid transferSplice variantsParkinson's disease pathogenesisVps13Lipid supplyMitochondriaMiroVPS13DERMESYeastMost lipidsTransport domainEukaryotesGem1MetazoansER
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
2015
SMP-domain proteins at membrane contact sites: Structure and function
Reinisch KM, De Camilli P. SMP-domain proteins at membrane contact sites: Structure and function. Biochimica Et Biophysica Acta 2015, 1861: 924-927. PMID: 26686281, PMCID: PMC4902782, DOI: 10.1016/j.bbalip.2015.12.003.Peer-Reviewed Original ResearchConceptsMembrane contact sitesContact sitesAnant K. MenonCellular lipid landscapeTim P. LevineER-mitochondrial contactsSMP domainLipid landscapeComplex subunitsPlasma membraneMolecular basisLipid transportersEndoplasmic reticulumProteinRecent discoveryMembraneSuch sitesSitesSubunitsReticulumTransportersGlycerolipidsRegulationElucidationSpecial issue
1999
Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein
Nemoto Y, De Camilli P. Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein. The EMBO Journal 1999, 18: 2991-3006. PMID: 10357812, PMCID: PMC1171381, DOI: 10.1093/emboj/18.11.2991.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBinding SitesCarrier ProteinsCHO CellsCloning, MolecularCricetinaeCytoplasmExonsIntracellular MembranesIsoenzymesMembrane ProteinsMitochondriaMolecular Sequence DataMutationNerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingRatsRecombinant Fusion ProteinsRNA, MessengerYeastsConceptsMitochondrial outer membrane proteinMitochondrial outer membraneOuter membrane proteinsPDZ domainMembrane proteinsSynaptojanin 2Outer membraneNovel mitochondrial outer membrane proteinC-terminal transmembrane regionSingle PDZ domainPerinuclear clusteringTransmembrane regionSynaptojanin 1C-terminusExon sequencesSpliced formsEnforced expressionUnique motifModulation of inositolIntracellular distributionSynaptic vesiclesMitochondriaPutative roleOmp25Protein