2018
Newly synthesized polycystin‐1 takes different trafficking pathways to the apical and ciliary membranes
Gilder AL, Chapin HC, Padovano V, Hueschen CL, Rajendran V, Caplan MJ. Newly synthesized polycystin‐1 takes different trafficking pathways to the apical and ciliary membranes. Traffic 2018, 19: 933-945. PMID: 30125442, PMCID: PMC6237641, DOI: 10.1111/tra.12612.Peer-Reviewed Original ResearchConceptsPolycystin-1Ciliary deliveryBrefeldin AApical deliveryRenal epithelial cellsN-terminal fragmentPolycystin-2LLC-PK1 renal epithelial cellsDifferent trafficking pathwaysTrans-Golgi networkApical membraneEpithelial cellsCultured epithelial cellsTrafficking pathwaysTransmembrane proteinGolgi compartmentPrimary ciliaC-terminal fragmentCiliary membraneC-terminusAutocatalytic cleavageDistinct pathwaysIncubating cellsCell membraneAutosomal dominant polycystic kidney disease
2015
Expression profiles of human epididymis epithelial cells reveal the functional diversity of caput, corpus and cauda regions
Browne JA, Yang R, Leir SH, Eggener SE, Harris A. Expression profiles of human epididymis epithelial cells reveal the functional diversity of caput, corpus and cauda regions. Molecular Human Reproduction 2015, 22: 69-82. PMID: 26612782, PMCID: PMC4733224, DOI: 10.1093/molehr/gav066.Peer-Reviewed Original ResearchConceptsCultured epithelial cellsEpididymis functionExpression profilesHuman epididymis epithelial cellsSperm maturationDefense response processNormal sperm maturationEpithelial cellsProcess enrichment analysisGene expression profilesLuminal environmentUrogenital tract developmentFunctional diversityTranscriptional profilingCauda cellsTranscription factorsBioinformatics toolsBiological replicatesMale genital ductsSimilar transcriptomesMolecular basisEnrichment analysisHormonal signalsSAMPLES/MATERIALSDifferential expressionAkt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia
Alves DS, Thulin G, Loffing J, Kashgarian M, Caplan MJ. Akt Substrate of 160 kD Regulates Na+,K+-ATPase Trafficking in Response to Energy Depletion and Renal Ischemia. Journal Of The American Society Of Nephrology 2015, 26: 2765-2776. PMID: 25788531, PMCID: PMC4625659, DOI: 10.1681/asn.2013101040.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiotinylationCell LineCytoplasmDogsDynaminsEndocytosisEpithelial CellsGTPase-Activating ProteinsHumansIschemiaKidneyKidney DiseasesMadin Darby Canine Kidney CellsMaleMiceMice, KnockoutMicroscopy, FluorescencePhosphorylationProtein TransportReperfusion InjuryRNA, Small InterferingSignal TransductionSodium-Potassium-Exchanging ATPaseConceptsRenal epithelial cellsATPase traffickingIntracellular compartmentsEpithelial cell polarityEpithelial cellsBasolateral plasma membraneGlucose transporter 4Cultured epithelial cellsCell polarityRab GTPaseAkt substratePlasma membraneSubcellular distributionAS160Energy depletionDirect bindingTransporter 4TraffickingDirect roleK-ATPaseATPaseTubular soluteIntracellular accumulationCellsCompartments
2012
AS160: a new Na,K‐ATPase partner that regulates the trafficking of the sodium pump in response to energy depletion and renal ischemia
Alves D, Thulin G, Loffing J, Kashgarian M, Caplan M. AS160: a new Na,K‐ATPase partner that regulates the trafficking of the sodium pump in response to energy depletion and renal ischemia. The FASEB Journal 2012, 26: lb808-lb808. DOI: 10.1096/fasebj.26.1_supplement.lb808.Peer-Reviewed Original ResearchPlasma membraneRenal epithelial cellsK-ATPaseEpithelial cellsCytoplasmic vesicular compartmentsDifferent cellular poolsCultured epithelial cellsVesicular compartmentsWild typeCellular poolAS160Cytoplasmic accumulationKnockout micePhysiological roleWild-type controlsEnergy depletionRenal ischemiaPhysiological stimuliType controlsCellular NaK-ATPase activityIntracellular accumulationMembraneIschemic kidney injuryCells
2009
Salmonella Typhimurium Type III Secretion Effectors Stimulate Innate Immune Responses in Cultured Epithelial Cells
Bruno VM, Hannemann S, Lara-Tejero M, Flavell RA, Kleinstein SH, Galán JE. Salmonella Typhimurium Type III Secretion Effectors Stimulate Innate Immune Responses in Cultured Epithelial Cells. PLOS Pathogens 2009, 5: e1000538. PMID: 19662166, PMCID: PMC2714975, DOI: 10.1371/journal.ppat.1000538.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsBlotting, WesternCell LineColitisEpithelial CellsGene ExpressionGene Expression ProfilingGuanine Nucleotide Exchange FactorsHumansImmunity, InnateMiceMitogen-Activated Protein Kinase KinasesMyotonin-Protein KinaseNF-kappa BOligonucleotide Array Sequence AnalysisProtein Serine-Threonine KinasesReverse Transcriptase Polymerase Chain ReactionSalmonella InfectionsSalmonella typhimuriumSignal TransductionTranscription, GeneticConceptsInnate immune receptorsInnate immune responseIntestinal inflammationImmune responseEpithelial cellsBacterial productsIntestinal inflammatory pathologyImmune receptorsCultured epithelial cellsEnteric pathogen Salmonella typhimuriumInnate immune systemIntestinal epithelial cellsInflammatory pathologyInflammatory responseType III secretion effectorsImmune systemSalmonella typhimuriumNF-kappaBMitogen-activated protein kinaseEnteric pathogensPathogen Salmonella typhimuriumPathologyReceptorsInflammationType III secretion system
2005
An indirect enzyme-linked immunosorbent assay for rapid and quantitative assessment of Type III virulence phenotypes of Pseudomonas aeruginosa isolates
Li L, Ledizet M, Kar K, Koski RA, Kazmierczak BI. An indirect enzyme-linked immunosorbent assay for rapid and quantitative assessment of Type III virulence phenotypes of Pseudomonas aeruginosa isolates. Annals Of Clinical Microbiology And Antimicrobials 2005, 4: 22. PMID: 16375761, PMCID: PMC1360672, DOI: 10.1186/1476-0711-4-22.Peer-Reviewed Original ResearchConceptsClinical isolatesEpithelial cellsOptimal treatment strategyLarge clinical studiesP. aeruginosa type III secretion systemP. aeruginosa isolatesEnzyme-linked immunosorbent assayEnzyme-linked immunosorbentType III secretion systemSecretion phenotypeIndirect enzyme-linked immunosorbentPseudomonas aeruginosaPoor outcomeInfected patientsIndirect enzyme-linked immunosorbent assayTreatment strategiesClinical studiesClinical diseaseSevere diseaseAeruginosa isolatesELISA assaysConclusionThe availabilityImmunosorbent assayCultured epithelial cellsVirulence factors
2004
Calcium Dependence of Polycystin-2 Channel Activity Is Modulated by Phosphorylation at Ser812 *
Cai Y, Anyatonwu G, Okuhara D, Lee KB, Yu Z, Onoe T, Mei CL, Qian Q, Geng L, Wiztgall R, Ehrlich BE, Somlo S. Calcium Dependence of Polycystin-2 Channel Activity Is Modulated by Phosphorylation at Ser812 *. Journal Of Biological Chemistry 2004, 279: 19987-19995. PMID: 14742446, DOI: 10.1074/jbc.m312031200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBiotinylationCalciumCasein Kinase IICell MembraneDNA, ComplementaryEndoplasmic ReticulumGenes, DominantGlutathione TransferaseGlycosylationMembrane ProteinsMiceMice, Inbred BALB CMicroscopy, FluorescenceMutationPhosphatesPhosphorylationPrecipitin TestsProtein Serine-Threonine KinasesProtein Structure, TertiaryReverse Transcriptase Polymerase Chain ReactionSerineTime FactorsTRPP Cation ChannelsConceptsPolycystin-2Non-phosphorylated formChannel activityCation channelsCultured epithelial cellsActivation/inactivationPolycystic kidney diseaseProtein phosphorylationSubstitution mutantsNon-selective cation channelsConstitutive phosphorylationDivalent cation channelsPolycystin-1Substrate domainEndoplasmic reticulumPhosphorylationSingle-channel studiesVivo analysisControl cellsEpithelial cellsAutosomal dominant polycystic kidney diseaseDominant polycystic kidney diseaseOpen probabilityCellsCK2
2001
INTERACTION OF BACTERIAL PATHOGENS WITH POLARIZED EPITHELIUM
Kazmierczak B, Mostov K, Engel J. INTERACTION OF BACTERIAL PATHOGENS WITH POLARIZED EPITHELIUM. Annual Review Of Microbiology 2001, 55: 407-435. PMID: 11544362, DOI: 10.1146/annurev.micro.55.1.407.Peer-Reviewed Original Research
2000
The Flagellar Sigma Factor FliA (ς28) Regulates the Expression of Salmonella Genes Associated with the Centisome 63 Type III Secretion System
Eichelberg K, Galán J. The Flagellar Sigma Factor FliA (ς28) Regulates the Expression of Salmonella Genes Associated with the Centisome 63 Type III Secretion System. Infection And Immunity 2000, 68: 2735-2743. PMID: 10768967, PMCID: PMC97482, DOI: 10.1128/iai.68.5.2735-2743.2000.Peer-Reviewed Original ResearchConceptsType III secretion systemSecretion systemExpression of componentsRegulatory proteinsType III protein secretion systemRegulatory mechanismsSerovar TyphimuriumFlagellar sigma factor FliASigma factor FliAProtein secretion systemTranscriptional regulatory proteinsSalmonella pathogenicity island 1Complex regulatory mechanismsFlagellar regulatory genesPathogenicity island 1Macrophage cell deathEffects of mutationsType III systemCultured epithelial cellsFlagellar genesEnterica serovar TyphimuriumMild centrifugal forceRegulatory genesSalmonella genesS. enterica serovar Typhimurium
1999
Pathogenicity Islands and the Evolution of Salmonella Virulence
Groisman E, Blanc‐Potard A, Uchiya K. Pathogenicity Islands and the Evolution of Salmonella Virulence. 1999, 127-150. DOI: 10.1128/9781555818173.ch7.Peer-Reviewed Original ResearchSPI-1 genesPathogenicity islandDNA segmentsSPI-1Evolution of SalmonellaCultured epithelial cellsSalmonella-specific sequenceTRNA genesExport apparatusTranscriptional unitsLarge operonNonhost environmentsSecretion systemBacterial entryHousekeeping genesSalmonella virulenceHost rangeSPI-2Secretory systemHost cellsAspects of infectionNonphagocytic cellsGenesMacrophage apoptosisOperonRequirement of p21-activated Kinase (PAK) for Salmonella typhimurium–induced Nuclear Responses
Chen L, Bagrodia S, Cerione R, Galán J. Requirement of p21-activated Kinase (PAK) for Salmonella typhimurium–induced Nuclear Responses. Journal Of Experimental Medicine 1999, 189: 1479-1488. PMID: 10224288, PMCID: PMC2193063, DOI: 10.1084/jem.189.9.1479.Peer-Reviewed Original ResearchConceptsP21-activated kinaseBacterial effector proteinsEffector proteinsTarget proteinsSmall molecular weight GTPasesSerine/threonine kinaseType III secretion systemCdc42 effector proteinsC-Jun NH2-terminal kinase activationCdc42/RacFunction of Cdc42PAK kinase activityDedicated type III secretion systemEffector loop mutantsActin cytoskeleton rearrangementActin cytoskeleton reorganizationHost cell cytoplasmCultured epithelial cellsNuclear responseWeight GTPasesThreonine kinaseRho familyRho GTPasesSecretion systemCytoskeletal rearrangements
1998
A substrate of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage
Hardt W, Urlaub H, Galán J. A substrate of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 2574-2579. PMID: 9482928, PMCID: PMC19418, DOI: 10.1073/pnas.95.5.2574.Peer-Reviewed Original ResearchConceptsType III protein secretion systemType III secretion systemProtein secretion systemSecretion systemEffector proteinsInvasion-associated type III secretion systemCluster of genesTail fiber proteinHost cell cytoplasmSouthern hybridization analysisMobile genetic elementsCultured epithelial cellsInduction of apoptosisSopE proteinEnterica serovar TyphimuriumBacteriophage genesBacterial entryCytoskeletal rearrangementsS. enterica serovar TyphimuriumGenetic elementsPathogenicity islandFiber proteinHybridization analysisCell cytoplasmEffector moleculesThe Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton
Fu Y, Galán J. The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Molecular Microbiology 1998, 27: 359-368. PMID: 9484891, DOI: 10.1046/j.1365-2958.1998.00684.x.Peer-Reviewed Original ResearchConceptsActin cytoskeletonHost cell actin cytoskeletonFusion proteinHost cellsAmino acidsAmino-terminal halfCell actin cytoskeletonCultured cells resultsWild-type toxinCultured epithelial cellsEffector proteinsModular domainsStress fibersActive GSTCytoskeletonProteinCells resultsEpithelial cellsGSTSPTPProlonged incubationTranslocationCellsS. typhimuriumMicroinjection
1996
Molecular genetic bases of Salmonella entry into host cells
Galán J. Molecular genetic bases of Salmonella entry into host cells. Molecular Microbiology 1996, 20: 263-271. PMID: 8733226, DOI: 10.1111/j.1365-2958.1996.tb02615.x.Peer-Reviewed Original ResearchConceptsMolecular genetic basisGenetic basisContact-dependent secretion systemsPlant pathogenic bacteriaNumber of proteinsNon-phagocytic cellsCultured epithelial cellsCentisome 63Secretion systemVariety of animalsKb regionSalmonella chromosomeSalmonella entryExtracellular environmentRemarkable homologyHost cellsEpithelial cellsEntry functionCellsChromosomesConsiderable progressHomologyLociOrganismsProteinChapter 6 The Spectrin Cytoskeleton and Organization of Polarized Epithelial Cell Membranes
Devarajan P, Morrow J. Chapter 6 The Spectrin Cytoskeleton and Organization of Polarized Epithelial Cell Membranes. Current Topics In Membranes 1996, 43: 97-128. DOI: 10.1016/s0070-2161(08)60386-x.Peer-Reviewed Original ResearchIntegral membrane proteinsPeripheral plasma membraneCultured epithelial cellsEpithelial cellsAnti-spectrin antibodiesEukaryotic cellsNonerythroid cellsMembrane proteinsSpectrin cytoskeletonEpithelial cell membranesPlasma membraneExperimental removalCell shapeDifferent isoformsMembrane stabilitySpectrinCell membraneCytoskeletonPostsynaptic densityPostsynaptic membraneMembrane instabilityCerebellar granule cellsSkeletal muscleMembraneCells
1994
The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins
Kaniga K, Bossio J, Galán J. The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins. Molecular Microbiology 1994, 13: 555-568. PMID: 7997169, DOI: 10.1111/j.1365-2958.1994.tb00450.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAraC Transcription FactorBacterial Outer Membrane ProteinsBacterial ProteinsBase SequenceCells, CulturedCloning, MolecularDNA-Binding ProteinsGene Expression Regulation, BacterialGenes, BacterialMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataMutagenesisRecombinant ProteinsRepressor ProteinsRestriction MappingSalmonella typhimuriumSequence Homology, Amino AcidTranscription FactorsTranscription, GeneticVirulenceConceptsCultured epithelial cellsSalmonella typhimurium genesNon-polar mutationT7 RNA polymerase-based expression systemEpithelial cellsAraC familyTranscription regulatorsInv locusTyphimurium genesNucleotide sequenceSalmonella entryInvGExpression systemInvFGenesProteinSequenceMutationsS. typhimuriumFamilyTranslocasesSimilar sizeCellsMembersHomologuesContact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium
Ginocchio C, Olmsted S, Wells C, Galán J. Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium. Cell 1994, 76: 717-724. PMID: 8124710, DOI: 10.1016/0092-8674(94)90510-x.Peer-Reviewed Original ResearchConceptsCultured epithelial cellsEpithelial cellsFormation of appendagesCell-signaling eventsDe novo protein synthesisNovo protein synthesisMembrane rufflesSurface organellesBacterial internalizationBacteria Salmonella typhimuriumSalmonella typhimuriumInternalization eventsSurface appendagesHost cellsNonphagocytic cellsS. typhimuriumProtein synthesisBacterial uptakeSuch appendagesSalmonella mutantsInternalization processIntimate interactionCellsBacteriaTyphimurium
1993
Signal transduction and invasion of epithelial cells by S. typhimurium
Pace J, Hayman M, Galán J. Signal transduction and invasion of epithelial cells by S. typhimurium. Cell 1993, 72: 505-514. PMID: 8382566, DOI: 10.1016/0092-8674(93)90070-7.Peer-Reviewed Original ResearchMeSH KeywordsArachidonate 5-LipoxygenaseArachidonic AcidCalciumCalcium-Calmodulin-Dependent Protein KinasesCells, CulturedEndocytosisEpidermal Growth FactorEpitheliumErbB ReceptorsPhospholipases APhospholipases A2PhosphorylationProtein KinasesSalmonella InfectionsSalmonella typhimuriumSignal TransductionSRS-AConceptsCultured epithelial cellsBacterial entryMitogen-activated protein kinaseEpithelial cellsS. typhimurium invasionS. typhimuriumEpidermal growth factor receptorSignal transductionProtein kinaseGrowth factor receptorHenle-407 cellsTyphimurium invasionHost cellsPathogenicity of SalmonellaFactor receptorInfected cellsMutantsInvasionCalcium fluxCellsPhospholipase A2TyphimuriumIntracellular calciumActivationFree intracellular calciumCloning and molecular characterization of a gene involved in Salmonella adherence and invasion of cultured epithelial cells
Altmeyer R, McNern J, Bossio JC, Rosenshine I, Finlay B, Galán J. Cloning and molecular characterization of a gene involved in Salmonella adherence and invasion of cultured epithelial cells. Molecular Microbiology 1993, 7: 89-98. PMID: 8382333, DOI: 10.1111/j.1365-2958.1993.tb01100.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial AdhesionBacterial ProteinsBase SequenceCells, CulturedDNA Transposable ElementsEpithelial CellsEpitheliumGenes, BacterialMolecular Sequence DataMutagenesisPhenotypeRecombinant Fusion ProteinsSalmonellaSalmonella typhimuriumSequence Homology, Nucleic AcidVirulenceConceptsCultured epithelial cellsInvH geneT7 RNA polymerase expression systemBacterial membrane fractionsEpithelial cellsSignal sequenceExtensive homologyColony hybridization analysisNucleotide sequenceGene productsHomologous sequencesExpression systemException of strainsMolecular characterizationGenesHybridization analysisMembrane fractionCultured cellsEscherichia coliPolypeptideInsertion sequence IS3E. coliOrganismsInvHSequence
1992
Involvement of the epidermal growth factor receptor in the invasion of cultured mammalian cells by Salmonella typhimurium
Galán J, Pace J, Hayman M. Involvement of the epidermal growth factor receptor in the invasion of cultured mammalian cells by Salmonella typhimurium. Nature 1992, 357: 588-589. PMID: 1608468, DOI: 10.1038/357588a0.Peer-Reviewed Original ResearchConceptsHenle-407 cellsEpidermal growth factor receptorMammalian cellsGrowth factor receptorTyrosine phosphorylationCultured mammalian cellsProtein tyrosine phosphorylationFactor receptorInternalization of SalmonellaCell surface receptorsCultured epithelial cellsAddition of EGFSuch phosphorylationSignal transductionSalmonella genesSalmonella typhimuriumEGF receptorS. typhimuriumIsogenic strainsEscherichia coliPhosphorylationEpithelial cellsGenesInternalizationInvasion
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