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
Salmonella entry into host cells: the work in concert of type III secreted effector proteins
Zhou D, Galán J. Salmonella entry into host cells: the work in concert of type III secreted effector proteins. Microbes And Infection 2001, 3: 1293-1298. PMID: 11755417, DOI: 10.1016/s1286-4579(01)01489-7.Peer-Reviewed Original ResearchConceptsActin cytoskeleton rearrangementCytoskeleton rearrangementActin dynamicsHost cellsHost actin dynamicsHost signal transductionType III secretion systemActin-binding proteinsSPI-1 type III secretion systemEffector proteinsSecretion systemSignal transductionActin rearrangementBacterial proteinsSalmonella entryIntestinal epithelial cellsBacterial uptakeCdc42Coordinated stepsProteinEpithelial cellsRacRearrangementCellsTransductionA 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, 40: 1461-1461. DOI: 10.1046/j.1365-2958.2001.02423.x.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
Striking a balance: Modulation of the actin cytoskeleton by Salmonella
Galán J, Zhou D. Striking a balance: Modulation of the actin cytoskeleton by Salmonella. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 8754-8761. PMID: 10922031, PMCID: PMC34008, DOI: 10.1073/pnas.97.16.8754.Peer-Reviewed Original ResearchConceptsType III secretion systemSecretion systemHost cellsBacterial entryGTP-binding protein Cdc42Bacterial effector proteinsInositol polyphosphate phosphatasePathogen/host relationshipActin cytoskeleton rearrangementHost cell cytosolStimulation of Cdc42Protein Cdc42Effector proteinsActin cytoskeletonExchange factorSpecialized organellesSalmonella proteinsCytoskeleton rearrangementT-plastinHost relationshipsCell cytosolF-actinCellular responsesG proteinsCdc42
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