2024
Rab6a enables BICD2/dynein-mediated trafficking of human papillomavirus from the trans-Golgi network during virus entry
Choi J, Speckhart K, Tsai B, DiMaio D. Rab6a enables BICD2/dynein-mediated trafficking of human papillomavirus from the trans-Golgi network during virus entry. MBio 2024, 15: e02811-24. PMID: 39431827, PMCID: PMC11559006, DOI: 10.1128/mbio.02811-24.Peer-Reviewed Original ResearchRab proteinsDNA virusesVirus entryHPV traffickingIntra-Golgi transportTrans-Golgi networkIntracellular vesicular transportMotor protein complexInfected cellsIntra-GolgiL2 capsid proteinRab GTPasesDynein adaptorsNon-enveloped DNA virusesRetrograde traffickingGolgi apparatusPotential targetProtein complexesVesicular transportRab6ADyneinTGNCapsid proteinRabCellular enzymes
2023
Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry
Choi J, DiMaio D. Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry. PLOS Pathogens 2023, 19: e1011648. PMID: 37703297, PMCID: PMC10519607, DOI: 10.1371/journal.ppat.1011648.Peer-Reviewed Original ResearchConceptsRetromer-mediated endosomeHPV entryGTP-bound formDominant negative Rab7Intracellular vesicular transportRetrograde transport pathwayVirus entryEndosomal exitRab GTPasesRab proteinsVesicle traffickingGolgi transportCellular proteinsVesicular transportProtein cargoKnockdown cellsIntracellular traffickingRab9AIncoming virusRab7EndosomesTraffickingTransport pathwaysProteinKey role
2022
Endoplasmic Reticulum Membrane Contact Sites, Lipid Transport, and Neurodegeneration.
Guillén-Samander A, De Camilli P. Endoplasmic Reticulum Membrane Contact Sites, Lipid Transport, and Neurodegeneration. Cold Spring Harbor Perspectives In Biology 2022, 15: a041257. PMID: 36123033, PMCID: PMC10071438, DOI: 10.1101/cshperspect.a041257.Peer-Reviewed Original ResearchConceptsMembrane contact sitesEndoplasmic reticulumEndoplasmic reticulum membrane contact sitesContact sitesLipid transportER membrane contact sitesCross talkLipid transfer proteinMutations of genesFamilial neurodegenerative diseasesIntracellular membranous organellesEndomembrane systemLipid trafficVesicular transportCell physiologyPlasma membraneMembranous organellesMembrane lipidsLipid exchangeTransfer proteinCell compartmentProteinNeurodegenerative diseasesMultiplicity of rolesDendritic tips
2020
Griscelli Syndrome Type 2 Sine Albinism: Unraveling Differential RAB27A Effector Engagement
Ohishi Y, Ammann S, Ziaee V, Strege K, Groß M, Amos C, Shahrooei M, Ashournia P, Razaghian A, Griffiths G, Ehl S, Fukuda M, Parvaneh N. Griscelli Syndrome Type 2 Sine Albinism: Unraveling Differential RAB27A Effector Engagement. Frontiers In Immunology 2020, 11: 612977. PMID: 33362801, PMCID: PMC7758216, DOI: 10.3389/fimmu.2020.612977.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdolescentAlbinismAnimalsBinding SitesCell LineChildChild, PreschoolChlorocebus aethiopsCOS CellsFemaleHumansInfantInfant, NewbornLeukocytes, MononuclearLymphohistiocytosis, HemophagocyticMaleMembrane ProteinsMutation, MissensePiebaldismPrimary Immunodeficiency Diseasesrab GTP-Binding Proteinsrab27 GTP-Binding ProteinsConceptsGS-2Rab GTPase familyRegulates vesicular transportAnimal cell linesGTPase familyOrganelle dynamicsTissue-specific effectorsVesicular transportMissense mutationsHemophagocytic lymphohistiocytosisCellular consequencesRab27aGriscelli syndrome type 2Episodes of hemophagocytic lymphohistiocytosisMutationsBinding sitesInborn errors of immunityCell linesPartial albinismErrors of immunityHair pigmentationCytotoxic lymphocytesClinical characteristicsInborn errorsAlbinismQuantitative Proteomic Analysis of Chikungunya Virus-Infected Aedes aegypti Reveals Proteome Modulations Indicative of Persistent Infection
Cui Y, Liu P, Mooney BP, Franz AWE. Quantitative Proteomic Analysis of Chikungunya Virus-Infected Aedes aegypti Reveals Proteome Modulations Indicative of Persistent Infection. Journal Of Proteome Research 2020, 19: 2443-2456. PMID: 32375005, PMCID: PMC7419016, DOI: 10.1021/acs.jproteome.0c00173.Peer-Reviewed Original ResearchConceptsSerine-type endopeptidasesMetabolism related pathwaysQuantitative proteomic analysisFunctional enrichment analysisChikungunya virusRibosome biogenesisLabel-free quantificationRNA machineryNonpathogenic relationshipsNovel proteinProteome modulationProteomic analysisVesicular transportEnrichment analysisCHIKV infectionOxidative phosphorylationBiological pathwaysRelated pathwaysMass spectrometry dataPresence of CHIKVProteinMosquito samplesProteomeOral acquisitionMolecular interactions
2019
Building sensory axons: Delivery and distribution of NaV1.7 channels and effects of inflammatory mediators
Akin EJ, Higerd-Rusli GP, Mis MA, Tanaka BS, Adi T, Liu S, Dib-Hajj FB, Waxman SG, Dib-Hajj SD. Building sensory axons: Delivery and distribution of NaV1.7 channels and effects of inflammatory mediators. Science Advances 2019, 5: eaax4755. PMID: 31681845, PMCID: PMC6810356, DOI: 10.1126/sciadv.aax4755.Peer-Reviewed Original ResearchConceptsMicrotubule-dependent vesicular transportSingle-molecule resolutionVesicular traffickingVesicular transportSurface deliveryPlasma membraneMembrane distributionFunctional studiesAxon terminiSodium channel NaLive visualizationSensory axonsVesiclesTraffickingNew insightsChannel NaContribution of NaDisease statesRab6ANav1.7 channelsDorsal root ganglion neuronsTerminusThreefold increaseGanglion neuronsMembraneSignal peptide peptidase‐like 2c impairs vesicular transport and cleaves SNARE proteins
Papadopoulou A, Müller S, Mentrup T, Shmueli M, Niemeyer J, Haug‐Kröper M, von Blume J, Mayerhofer A, Feederle R, Schröder B, Lichtenthaler S, Fluhrer R. Signal peptide peptidase‐like 2c impairs vesicular transport and cleaves SNARE proteins. EMBO Reports 2019, 20: embr201846451. PMID: 30733281, PMCID: PMC6399617, DOI: 10.15252/embr.201846451.Peer-Reviewed Original ResearchMeSH KeywordsAcrosomeAnimalsAspartic Acid EndopeptidasesBiocatalysisDown-RegulationGlycomicsGlycoproteinsGlycosyltransferasesGolgi ApparatusHEK293 CellsHumansMaleMembrane ProteinsMice, Inbred C57BLModels, BiologicalProtein TransportProteolysisSNARE ProteinsSpermatidsSubcellular FractionsSubstrate SpecificityConceptsSNARE proteinsCandidate substratesVesicular transportProcess of vesicular traffickingImpaired vesicular transportIntramembrane aspartyl proteaseCleave SNARE proteinsGxGD-typeAcrosome formationB cell developmentCargo proteinsVesicular traffickingAspartyl proteaseProtease familyCellular processesProtein glycosylationSubcellular compartmentsEndoplasmic reticulumProteolytic processingBiological processesAlzheimer's diseasePhysiological functionsProteinDevelopment of pathologyProtease
2018
Chapter 39 Structure-Function Relationships in the Pancreatic Acinar Cell
Gorelick F, Pandol S, Jamieson J. Chapter 39 Structure-Function Relationships in the Pancreatic Acinar Cell. 2018, 869-894. DOI: 10.1016/b978-0-12-809954-4.00039-6.Peer-Reviewed Original ResearchProtein synthesisEnzyme precursorsRodent acinar cellsAcinar cellsZymogen granulesCritical physiologic functionsSecretion of enzymesStructure-function relationshipsMajor cell typesCellular functionsCell biologistsVesicular transportCell signalingGolgi complexHuman acinar cellsPhysiologic functionEndoplasmic reticulumDuct cellsCell organellesPancreatic acinar cellsCell typesEnzyme proteinDigestive enzymesEnzymeMajor physiologic function
2017
Differential requirement for N‐ethylmaleimide‐sensitive factor in endosomal trafficking of transferrin receptor from anterograde trafficking of vesicular stomatitis virus glycoprotein G
Fan J, Zhou X, Wang Y, Kuang C, Sun Y, Liu X, Toomre D, Xu Y. Differential requirement for N‐ethylmaleimide‐sensitive factor in endosomal trafficking of transferrin receptor from anterograde trafficking of vesicular stomatitis virus glycoprotein G. FEBS Letters 2017, 591: 273-281. PMID: 27995606, DOI: 10.1002/1873-3468.12532.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoprotein GGolgi structureDifferential requirementN-ethylmaleimide-sensitive factorConstitutive trafficking pathwayTrafficking pathwaysGlycoprotein GTransferrin endocytosisEndosomal traffickingAnterograde traffickingGolgi fragmentationMammalian cellsVesicular transportDifferent vesiclesHeLa cellsReceptor exocytosisTraffickingTransferrin receptorFusion factorKnockdownCell viabilityCentral rolePathwayCrucial roleCells
2016
Extended‐Synaptotagmins as Lipid Transporters at ER‐PM Contact Sites
Reinisch K, Schauder C, Wu X, Saheki Y, Narayanaswamy P, Torta F, Wenk M, De Camilli P. Extended‐Synaptotagmins as Lipid Transporters at ER‐PM Contact Sites. The FASEB Journal 2016, 30 DOI: 10.1096/fasebj.30.1_supplement.115.2.Peer-Reviewed Original ResearchMembrane contact sitesSMP domainContact sitesExtended synaptotagminsEndoplasmic reticulumPlasma membraneER-PM contact sitesLipid transportLipid transferLipid-binding modulesER-PM tethersΒ-barrel structureExchange of lipidsERMES complexE-SytsProtein modulesProtein domainsVesicular transportC2 domainÅ resolutionLipid transportersHydrophobic residuesUehara Memorial FoundationSynaptotagmin 2Direct roleSelf-assembly of size-controlled liposomes on DNA nanotemplates
Yang Y, Wang J, Shigematsu H, Xu W, Shih WM, Rothman JE, Lin C. Self-assembly of size-controlled liposomes on DNA nanotemplates. Nature Chemistry 2016, 8: 476-483. PMID: 27102682, PMCID: PMC5021307, DOI: 10.1038/nchem.2472.Peer-Reviewed Original ResearchConceptsDNA nanotemplatesArtificial lipid bilayer membranesLipid bilayer formationLipid bilayer membranesSelf-AssemblyTemplating methodKey intermediateBilayer formationDrug deliveryArtificial vesiclesLipid compositionNanoscale precisionNanotemplatesHomogeneous liposomesUnilamellar vesiclesLiposome formationVesicular transportProtein structureMembrane structureVesicle sizeLiposomesIntermediatesFormationVesiclesStructure
2015
Direct Binding of Retromer to Human Papillomavirus Type 16 Minor Capsid Protein L2 Mediates Endosome Exit during Viral Infection
Popa A, Zhang W, Harrison MS, Goodner K, Kazakov T, Goodwin EC, Lipovsky A, Burd CG, DiMaio D. Direct Binding of Retromer to Human Papillomavirus Type 16 Minor Capsid Protein L2 Mediates Endosome Exit during Viral Infection. PLOS Pathogens 2015, 11: e1004699. PMID: 25693203, PMCID: PMC4334968, DOI: 10.1371/journal.ppat.1004699.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkRetromer cargoTransmembrane proteinGolgi apparatusDirect bindingCoat protein complexCellular transmembrane proteinsVirus entryMinor capsid proteinCarboxy-terminal segmentProtein complexesL2 minor capsid proteinMinor capsid protein L2Early endosomesVesicular transportRetromerPlasma membraneEndosomal membranesBinding motifProtein L2Capsid proteinEndosomesL2 proteinViral componentsProtein
2012
Chapter 49 Structure–function Relationships in the Pancreatic Acinar Cell
Gorelick F, Jamieson J. Chapter 49 Structure–function Relationships in the Pancreatic Acinar Cell. 2012, 1341-1360. DOI: 10.1016/b978-0-12-382026-6.00049-x.Peer-Reviewed Original ResearchProtein synthesisZymogen granulesAcinar cellsSecretion of enzymesStructure-function relationshipsNascent proteinsVesicular transportCell signalingEnzyme precursorsGolgi complexEndoplasmic reticulumPancreatic acinar cellsDigestive enzymesEnzymeModel systemExport protein synthesisVectorial mannerApical regionProteinCellsHormonal routesGranulesDigestionDietary proteinExocytosis
2008
Ankyrin Repeat Proteins Comprise a Diverse Family of Bacterial Type IV Effectors
Pan X, Lührmann A, Satoh A, Laskowski-Arce MA, Roy CR. Ankyrin Repeat Proteins Comprise a Diverse Family of Bacterial Type IV Effectors. Science 2008, 320: 1651-1654. PMID: 18566289, PMCID: PMC2514061, DOI: 10.1126/science.1158160.Peer-Reviewed Original ResearchConceptsSecretion systemL. pneumophila-containing vacuoleIntracellular pathogen Legionella pneumophilaHost cellsDifferent bacterial proteinsType IV secretion systemMicrotubule-dependent vesicular transportEukaryotic host cellsType IV effectorsPathogen Legionella pneumophilaSpecialized secretion systemsAnkyrin Repeat ProteinsANK proteinsEukaryotic cellsHomology domainEffector proteinsEukaryotic factorsRepeat proteinsInfection of macrophagesVesicular transportBacterial proteinsLate endosomesDiverse familyProteinLegionella pneumophila
2006
The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor
Murata T, Delprato A, Ingmundson A, Toomre DK, Lambright DG, Roy CR. The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nature Cell Biology 2006, 8: 971-977. PMID: 16906144, DOI: 10.1038/ncb1463.Peer-Reviewed Original ResearchConceptsGuanine nucleotide exchange factorsNucleotide exchange factorsType IV secretion apparatusIntracellular pathogen Legionella pneumophilaHost cellsEndoplasmic reticulum-derived vesiclesDot/IcmPathogen Legionella pneumophilaL. pneumophila mutantsRab1 recruitmentSubstrate proteinsRab familyExchange factorGTPase Rab1Secretion apparatusVesicular transportBacterial proteinsGolgi apparatusVisual screenEndoplasmic reticulumRab1Membrane transportSpecific membersDrrAIntracellular pathogensRab33A: Characterization, Expression, and Suppression by Epigenetic Modification
Cheng E, Trombetta SE, Kovacs D, Beech RD, Ariyan S, Reyes-Mugica M, McNiff JM, Narayan D, Kluger HM, Picardo M, Halaban R. Rab33A: Characterization, Expression, and Suppression by Epigenetic Modification. Journal Of Investigative Dermatology 2006, 126: 2257-2271. PMID: 16810302, DOI: 10.1038/sj.jid.5700386.Peer-Reviewed Original ResearchConceptsX chromosome-linked geneSpecific gene expressionTranscription initiation siteSpecific promoter regionsMelanoma cellsGTPase mutantsEpigenetic modificationsSmall GTPaseDNA methylationVesicular transportRab33AGene expressionPromoter regionMelanosomal proteinsInitiation siteNormal melanocytesAberrant downregulationGenesEarly eventsAberrant processesMelanocytesExpressionGTPaseImportant roleNormal process
2005
Early Transcriptional Response of Human Neutrophils to Anaplasma phagocytophilum Infection
Sukumaran B, Carlyon JA, Cai JL, Berliner N, Fikrig E. Early Transcriptional Response of Human Neutrophils to Anaplasma phagocytophilum Infection. Infection And Immunity 2005, 73: 8089-8099. PMID: 16299303, PMCID: PMC1307096, DOI: 10.1128/iai.73.12.8089-8099.2005.Peer-Reviewed Original ResearchConceptsEarly transcriptional responseTranscriptional responseGene expressionHost cell gene expressionComprehensive DNA microarray analysisA. phagocytophilum infectionDNA microarray analysisObligate intracellular pathogensCell gene expressionCFLAR geneTNFSF10 geneA. phagocytophilum-infected neutrophilsCytoskeletal remodelingVesicular transportTranscriptional profilesHost pathwaysMicroarray analysisAntiapoptotic genesPromyelocytic cell lineDifferential expressionPhagocytophilum infectionHost cellsGenesHuman neutrophilsIntracellular pathogens
2003
A General Role for Rab27a in Secretory Cells
Tolmachova T, Anders R, Stinchcombe J, Bossi G, Griffiths G, Huxley C, Seabra M. A General Role for Rab27a in Secretory Cells. Molecular Biology Of The Cell 2003, 15: 332-344. PMID: 14617806, PMCID: PMC307551, DOI: 10.1091/mbc.e03-07-0452.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedEndocrine GlandsExocrine GlandsExocytosisFemaleGastrointestinal TractGene Expression RegulationGreen Fluorescent ProteinsImmunohistochemistryLuminescent ProteinsMiceMice, TransgenicMicroscopy, ElectronOvaryrab GTP-Binding Proteinsrab27 GTP-Binding Proteinsrab3 GTP-Binding ProteinsRecombinant Fusion ProteinsTissue DistributionConceptsSecretory cellsComplex pattern of expressionSpecialized secretory cellsFunction of proteinsCell-specific expressionSpecialized cell typesRab3 proteinsPattern of expressionRab GTPasesVesicular transportComplex multistep processFusion proteinRab27aMammalian organismsSecretory eventsCell typesProteinMultistep processGeneral roleHematopoietic cellsKnockout miceCellsComplex patternsRab3GTPase
2000
Molecular motors: the driving force behind mammalian left–right development
Supp D, Potter S, Brueckner M, Supp D, Potter S, Brueckner M. Molecular motors: the driving force behind mammalian left–right development. Trends In Cell Biology 2000, 10: 41-45. PMID: 10652513, DOI: 10.1016/s0962-8924(99)01701-8.Peer-Reviewed Original ResearchConceptsEarly vertebrate developmentMitotic spindle movementsLarge protein complexesLeft-right developmentLeft-right axisEmbryonic patterningVertebrate developmentProtein complexesCellular processesMicrotubule cytoskeletonVesicular transportSpindle movementsATP hydrolysisMolecular motorsDirectional movementCiliary beatingUnique roleCytoskeletonKinesinPatterningComplexesHydrolysis
1996
Phosphoinositides as Regulators in Membrane Traffic
De Camilli P, Emr S, McPherson P, Novick P. Phosphoinositides as Regulators in Membrane Traffic. Science 1996, 271: 1533-1539. PMID: 8599109, DOI: 10.1126/science.271.5255.1533.Peer-Reviewed Original ResearchConceptsMembrane trafficActivation of proteinsGuanosine triphosphatasesSignal transductionVesicular transportRegulatory mechanismsPhosphatidylinositol metabolitesSecond messengerLocation signalPhosphorylated productsCell surfaceClassical rolePhosphoinositideCritical rolePhosphatidylinositolTransductionTriphosphatasesRegulatorProteinMessengerRegulationPolar headRoleRecruitmentActivation
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