2006
Differential activation and function of Rho GTPases during Salmonella–host cell interactions
Patel JC, Galán J. Differential activation and function of Rho GTPases during Salmonella–host cell interactions. Journal Of Cell Biology 2006, 175: 453-463. PMID: 17074883, PMCID: PMC2064522, DOI: 10.1083/jcb.200605144.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBacterial ProteinsCdc42 GTP-Binding ProteinCell MembraneChlorocebus aethiopsCOS CellsEnzyme ActivationGuanine Nucleotide Exchange FactorsHumansIntestinal MucosaMutationRac1 GTP-Binding ProteinRho GTP-Binding ProteinsRNA InterferenceSalmonella InfectionsSalmonella typhimuriumTransfectionConceptsRho family GTPasesExchange factorCellular responsesRho family guanosine triphosphatasesSalmonella-host cell interactionsType III secretion systemSpecific Rho family GTPasesActin cytoskeleton remodelingDifferent Rho family GTPasesSpecific cellular responsesActin remodelingGuanosine triphosphatasesRho GTPasesSecretion systemCytoskeleton remodelingBacterial proteinsGTPasesSophisticated mechanismsHost cellsDistinct rolesBacterial pathogensCell interactionsSalmonella entericaDifferential activationCentral role
2004
Salmonella Modulates Vesicular Traffic by Altering Phosphoinositide Metabolism
Hernandez LD, Hueffer K, Wenk MR, Galán J. Salmonella Modulates Vesicular Traffic by Altering Phosphoinositide Metabolism. Science 2004, 304: 1805-1807. PMID: 15205533, DOI: 10.1126/science.1098188.Peer-Reviewed Original ResearchConceptsIntracellular replicative nicheType III secretion systemActin cytoskeleton rearrangementBacteria-containing vacuolesBacterial intracellular growthPhosphoinositide phosphataseInnate immune defenseSecretion systemReplicative nicheBacterial entryCytoskeleton rearrangementSpacious phagosomesHost cellsNonphagocytic cellsIntracellular growthImmune defenseSopBPhosphoinositide metabolismSignificant defectsSalmonella entericaVacuolesMembraneCellsNichePhagosomes
2001
Genetic Analysis of Assembly of theSalmonella enterica Serovar Typhimurium Type III Secretion-Associated Needle Complex
Sukhan A, Kubori T, Wilson J, Galán J. Genetic Analysis of Assembly of theSalmonella enterica Serovar Typhimurium Type III Secretion-Associated Needle Complex. Journal Of Bacteriology 2001, 183: 1159-1167. PMID: 11157927, PMCID: PMC94988, DOI: 10.1128/jb.183.4.1159-1167.2001.Peer-Reviewed Original ResearchA Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
Zhou D, Chen L, Hernandez L, Shears S, Galán J. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Molecular Microbiology 2001, 39: 248-260. PMID: 11136447, DOI: 10.1046/j.1365-2958.2001.02230.x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBacterial ProteinsCdc42 GTP-Binding ProteinCell MembraneCells, CulturedChlorocebus aethiopsCOS CellsCytoskeletonHumansInositol PhosphatesIntestinesJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesPhosphoric Monoester HydrolasesPhosphorylationSalmonella InfectionsSalmonella typhimuriumTransfectionConceptsActin cytoskeleton rearrangementCytoskeleton rearrangementBacterial entrySecretion systemBacterial internalizationCellular responsesHost cellsRho GTPases signalingProtein secretion systemHost cell actin cytoskeleton rearrangementsHost cellular functionsSpecialized protein secretion systemCdc42-dependent mannerNon-phagocytic cellsBacterial effectorsAbility of SalmonellaInositol phosphataseCellular functionsDefective mutantsBacterial proteinsCo-ordinated functionSalmonella pathogenicityBacterium's abilitySopBPhospholipase C.
2000
Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
Kubori T, Sukhan A, Aizawa S, Galán J. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 10225-10230. PMID: 10944190, PMCID: PMC27824, DOI: 10.1073/pnas.170128997.Peer-Reviewed Original ResearchConceptsType III secretion systemProtein secretion systemSecretion systemNeedle complexType III protein secretion systemHost cellular functionsSpecialized protein secretion systemType III secretion export apparatusType III secretionPathogenicity island 1Secretion complexPathogen's benefitExport apparatusCellular functionsAnimal cellsNeedle-like projectionsBacterial proteinsBacterium's abilityNeedle substructureIsland 1Host cellsMolecular characterizationNonphagocytic cellsNeedle componentBacterial pathogens
1999
A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
Fu Y, Galán J. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 1999, 401: 293-297. PMID: 10499590, DOI: 10.1038/45829.Peer-Reviewed Original ResearchMeSH KeywordsActinsArginineBacterial AdhesionBacterial ProteinsCdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsCell MembraneEscherichia coliGTPase-Activating ProteinsGTP-Binding ProteinsHumansJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesMutationProtein KinasesProtein Tyrosine PhosphatasesProteinsRecombinant Fusion ProteinsSalmonella typhimuriumConceptsHost cell cytosolActin cytoskeletonType III secretion systemProtein secretion systemSpecialized protein secretion systemActin cytoskeleton reorganizationCell actin cytoskeletonActin cytoskeletal changesRho GTPase proteinsRac-1Bacterial effectorsEffector proteinsExchange factorGTPase proteinsSecretion systemSalmonella proteinsCytoskeletal changesCellular responsesCdc42ProteinInfected cellsBacterial invasionCytosolBacteriumSPTPRole of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization
Zhou D, Mooseker M, Galán J. Role of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization. Science 1999, 283: 2092-2095. PMID: 10092234, DOI: 10.1126/science.283.5410.2092.Peer-Reviewed Original Research
1998
S. typhimurium Encodes an Activator of Rho GTPases that Induces Membrane Ruffling and Nuclear Responses in Host Cells
Hardt W, Chen L, Schuebel K, Bustelo X, Galán J. S. typhimurium Encodes an Activator of Rho GTPases that Induces Membrane Ruffling and Nuclear Responses in Host Cells. Cell 1998, 93: 815-826. PMID: 9630225, DOI: 10.1016/s0092-8674(00)81442-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCalcium-Calmodulin-Dependent Protein KinasesCdc42 GTP-Binding ProteinCell Cycle ProteinsCell MembraneCell NucleusCOS CellsCytoskeletonEnzyme ActivationGTP PhosphohydrolasesGTPase-Activating ProteinsGTP-Binding ProteinsGuanosine DiphosphateGuanosine TriphosphateHeLa CellsHumansJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein KinasesProteinsSalmonella typhimuriumSignal TransductionConceptsHost cellsMembrane rufflingSecretion systemGDP/GTP nucleotide exchangeProtein secretion systemActivator of RhoCDNA library screenActin cytoskeleton rearrangementRac-1Rho GTPasesCytoskeletal reorganizationCytoskeleton rearrangementBacterial proteinsNucleotide exchangeLibrary screenJNK activationCellular responsesNuclear responseCdc42Pathogen inducesSopERufflingMicrobial stimulationProteinCellsSupramolecular Structure of the Salmonella typhimurium Type III Protein Secretion System
Kubori T, Matsushima Y, Nakamura D, Uralil J, Lara-Tejero M, Sukhan A, Galán J, Aizawa S. Supramolecular Structure of the Salmonella typhimurium Type III Protein Secretion System. Science 1998, 280: 602-605. PMID: 9554854, DOI: 10.1126/science.280.5363.602.Peer-Reviewed Original Research
1994
The molecular genetic bases of Salmonella entry into mammalian cells
Galán J, Ginocchio C. The molecular genetic bases of Salmonella entry into mammalian cells. Biochemical Society Transactions 1994, 22: 301-306. PMID: 7958312, DOI: 10.1042/bst0220301.Peer-Reviewed Original Research