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 rolePathogenic RAB34 variants impair primary cilium assembly and cause a novel oral-facial-digital syndrome
Bruel A, Ganga A, Nosková L, Valenzuela I, Martinovic J, Duffourd Y, Zikánová M, Majer F, Kmoch S, Mohler M, Sun J, Sweeney L, Martínez-Gil N, Thauvin-Robinet C, Breslow D. Pathogenic RAB34 variants impair primary cilium assembly and cause a novel oral-facial-digital syndrome. Human Molecular Genetics 2023, 32: 2822-2831. PMID: 37384395, PMCID: PMC10481091, DOI: 10.1093/hmg/ddad109.Peer-Reviewed Original ResearchConceptsCilia assemblyCiliary membrane formationIntracellular ciliogenesis pathwayPrimary cilia assemblyBi-allelic missense variantsRab proteinsRab GTPaseCiliary proteinsSmall GTPaseNascent ciliaMother centriolePrimary ciliaC-terminusProtein productsPathogenic variantsRab34Cell typesFunctional impactMissense variantsGTPaseStrong lossCiliogenesisSignificant defectsGenesKey mediator
2010
The Stress Hormone Corticosterone Increases Synaptic α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors via Serum- and Glucocorticoid-inducible Kinase (SGK) Regulation of the GDI-Rab4 Complex*
Liu W, Yuen EY, Yan Z. The Stress Hormone Corticosterone Increases Synaptic α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors via Serum- and Glucocorticoid-inducible Kinase (SGK) Regulation of the GDI-Rab4 Complex*. Journal Of Biological Chemistry 2010, 285: 6101-6108. PMID: 20051515, PMCID: PMC2825404, DOI: 10.1074/jbc.m109.050229.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Inflammatory AgentsCell LineCerebral CortexCorticosteroneGuanine Nucleotide Dissociation InhibitorsImmediate-Early ProteinsMiceNeuronsProtein Serine-Threonine KinasesProtein Transportrab4 GTP-Binding ProteinsRatsReceptors, AMPAReceptors, NeurotransmitterSynapsesUp-RegulationConceptsNucleotide Dissociation InhibitorSer-213Glucocorticoid-inducible kinaseRab proteinsKinase regulationDissociation inhibitorIsoxazolepropionic acid (AMPA) receptorsSmall GTPaseEarly endosomesAcid receptorsFunctional cycleCorticosteroid signalingSGK phosphorylationPlasma membraneRab4Receptor recyclingMolecular mechanismsCellular targetsCorticosteroid stress hormonesNeuronal functionPhosphorylationSurface expressionStress hormonesMembraneRegulation
2007
Legionella pneumophila proteins that regulate Rab1 membrane cycling
Ingmundson A, Delprato A, Lambright DG, Roy CR. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 2007, 450: 365-369. PMID: 17952054, DOI: 10.1038/nature06336.Peer-Reviewed Original ResearchConceptsDrrA proteinRab1 functionMembrane cyclingGTPase-activating protein activityIntracellular pathogen Legionella pneumophilaRecruitment of Rab1Pathogen-occupied vacuolesPathogen Legionella pneumophilaDistinct biochemical reactionsL. pneumophilaLegionella pneumophilaRab1 activityRab1 activationRab proteinsEukaryotic cellsExchange factorGTP hydrolysisProtein activityRab1Membrane functionBacterial replicationProteinBiochemical reactionsPneumophilaVacuoles
2002
Secretory lysosomes
Blott E, Griffiths G. Secretory lysosomes. Nature Reviews Molecular Cell Biology 2002, 3: 122-131. PMID: 11836514, DOI: 10.1038/nrm732.Peer-Reviewed Original ResearchConceptsSecretory lysosomesConventional lysosomesStorage of secretory proteinsProtein sorting pathwayMechanism of secretionPopulation of lysosomesRab proteinsSecretion machinerySorting pathwayUnique organelleSecretory proteinsGene productsModified lysosomesLysosomal biogenesisOrganellesSecretory granulesGenetic diseasesLysosomal functionLysosomesChediak-HigashiSecretory productsHermansky-PudlakGenetic disordersSecretory mechanismHaematopoietic lineages
2001
Rab27a Is Required for Regulated Secretion in Cytotoxic T Lymphocytes
Stinchcombe J, Barral D, Mules E, Booth S, Hume A, Machesky L, Seabra M, Griffiths G. Rab27a Is Required for Regulated Secretion in Cytotoxic T Lymphocytes. Journal Of Cell Biology 2001, 152: 825-834. PMID: 11266472, PMCID: PMC2195783, DOI: 10.1083/jcb.152.4.825.Peer-Reviewed Original ResearchMeSH KeywordsActin-Related Protein 2Actin-Related Protein 3ActinsAnimalsbeta-N-AcetylhexosaminidasesCathepsin DCell MembraneCell PolarityCytoplasmic GranulesCytoskeletal ProteinsGolgi ApparatusGranzymesHermanski-Pudlak SyndromeHypopigmentationImmunologic Deficiency SyndromesMiceMice, Inbred C3HMice, Inbred C57BLMice, Mutant Strainsrab GTP-Binding Proteinsrab27 GTP-Binding ProteinsSecretory VesiclesSerine EndopeptidasesT-Lymphocytes, CytotoxicTalinConceptsCytotoxic T lymphocytesKill target cellsImmunological synapseT lymphocytesRab geranylgeranyl transferaseTarget cellsAshen (ashLoss of function mutationsActivation of RabsSecrete granzyme ARab proteinsMembrane dockingMouse models of human diseaseAshen miceRab27a activityGeranylgeranyl transferaseModels of human diseaseRab27aRegulate secretionFunction mutationsRAB27A geneGranzyme AHuman diseasesLytic granulesMouse model
1999
Molecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*
Luan P, Balch W, Emr S, Burd C. Molecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*. Journal Of Biological Chemistry 1999, 274: 14806-14817. PMID: 10329679, DOI: 10.1074/jbc.274.21.14806.Peer-Reviewed Original ResearchConceptsRecycling factorNucleotide Dissociation InhibitorFusion of vesiclesSite-directed mutagenesisAmino acid residuesRab deliveryDistinct RabsRab GTPasesRab proteinsRab-GDPDissociation inhibitorMembrane associationEssential proteinsMolecular dissectionEndocytic pathwayGDI functionAcid residuesRabCellular membranesDominant inhibitionMultiple effectorsRate of recyclingInhibitor functionProteinEndogenous pool
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