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
2014
Coupling between endocytosis and sphingosine kinase 1 recruitment
Shen H, Giordano F, Wu Y, Chan J, Zhu C, Milosevic I, Wu X, Yao K, Chen B, Baumgart T, Sieburth D, De Camilli P. Coupling between endocytosis and sphingosine kinase 1 recruitment. Nature Cell Biology 2014, 16: 652-662. PMID: 24929359, PMCID: PMC4230894, DOI: 10.1038/ncb2987.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCaenorhabditisCell MembraneCells, CulturedChlorocebus aethiopsCholesterolCOS CellsEndocytosisFluorescent Antibody TechniqueHEK293 CellsHeLa CellsHumansMiceModels, MolecularMutationPhosphotransferases (Alcohol Group Acceptor)Protein BindingProtein Structure, TertiarySequence AnalysisConceptsSphingosine kinase 1Hydrophobic patchN-BAR proteinsEndocytic membrane trafficExo/endocytosisPlasma membrane resultsMembrane trafficEndocytic intermediatesFunction mutantsMembrane recruitmentEndocytic membranesCellular compartmentsIntercellular signalingRecycling defectsSphingosine phosphorylationKinase 1Genetic studiesFunctional linkTubular invaginationsSphingolipid metabolismLipid bilayersEndocytosisEnzyme surfaceMembrane resultsRecruitment
2010
Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin
Shen H, Ferguson SM, Dephoure N, Park R, Yang Y, Volpicelli-Daley L, Gygi S, Schlessinger J, De Camilli P. Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin. Molecular Biology Of The Cell 2010, 22: 493-502. PMID: 21169560, PMCID: PMC3038647, DOI: 10.1091/mbc.e10-07-0637.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCdc42 GTP-Binding ProteinCell LineChlorocebus aethiopsClathrinClathrin Heavy ChainsClathrin Light ChainsCoated Pits, Cell-MembraneCOS CellsDynamin IDynamin IIEndocytosisFibroblastsGene Knockout TechniquesHumansMiceMice, KnockoutPhosphorylationProtein BindingProtein-Tyrosine KinasesSignal TransductionConceptsEndocytic clathrin-coated pitsClathrin-coated pitsRNA interference-based approachesFundamental cellular processesGrowth factor receptor signalingWild-type cellsNonreceptor tyrosine kinaseActive Cdc42Cellular processesSpecific cargoClathrin assemblyEndocytic routeEndocytic vesiclesGrowth factor receptorTyrosine phosphorylationPhosphorylation stateClathrin boxTyrosine kinaseKinase phosphorylationCdc42Receptor signalingActivation-deactivation cyclePhosphorylationDynaminFactor receptor