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
2003
A Salmonella protein causes macrophage cell death by inducing autophagy
Hernandez LD, Pypaert M, Flavell RA, Galán J. A Salmonella protein causes macrophage cell death by inducing autophagy. Journal Of Cell Biology 2003, 163: 1123-1131. PMID: 14662750, PMCID: PMC2173598, DOI: 10.1083/jcb.200309161.Peer-Reviewed Original ResearchConceptsMembrane fusion activityCell deathType III protein secretion systemFusion activityProtein secretion systemMacrophage cell deathEndoplasmic reticulum markerSalmonella-infected macrophagesSecretion systemSalmonella proteinsAutophagic vesiclesMutant formsSipBHost cellsCultured cellsMitochondriaMembrane structureSalmonella entericaProteinCausative agentMarked accumulationMacrophagesCellsAutophagosomesAutophagy
2001
A 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
A Bacterial Toxin That Controls Cell Cycle Progression as a Deoxyribonuclease I-Like Protein
Lara-Tejero M, Galán J. A Bacterial Toxin That Controls Cell Cycle Progression as a Deoxyribonuclease I-Like Protein. Science 2000, 290: 354-357. PMID: 11030657, DOI: 10.1126/science.290.5490.354.Peer-Reviewed Original ResearchConceptsCell cycle arrestCytolethal distending toxinChromatin disruptionCycle arrestCell cycle progressionLike proteinCdtB mutantChromatin fragmentationTransient expressionMutant formsCycle progressionCell deathCDT holotoxinDistending toxinCultured cellsBacterial toxinsDeoxyribonuclease IBacterial pathogensSuch pathogensCdtBSubunitsCampylobacter jejuniToxinMorphological changesPathogens
1999
Requirement 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
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 stimulationProteinCells
1996
Requirement of CDC42 for Salmonella-Induced Cytoskeletal and Nuclear Responses
Chen L, Hobbie S, Galán J. Requirement of CDC42 for Salmonella-Induced Cytoskeletal and Nuclear Responses. Science 1996, 274: 2115-2118. PMID: 8953049, DOI: 10.1126/science.274.5295.2115.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein KinasesCdc42 GTP-Binding ProteinCell Cycle ProteinsCell NucleusCOS CellsCytoskeletonEnzyme ActivationGTP-Binding ProteinsJNK Mitogen-Activated Protein KinasesMitogen-Activated Protein KinasesPinocytosisRac GTP-Binding ProteinsSalmonella typhimuriumSignal TransductionTransfection