2023
Parkinson’s disease kinase LRRK2 coordinates a cell-intrinsic itaconate-dependent defence pathway against intracellular Salmonella
Lian H, Park D, Chen M, Schueder F, Lara-Tejero M, Liu J, Galán J. Parkinson’s disease kinase LRRK2 coordinates a cell-intrinsic itaconate-dependent defence pathway against intracellular Salmonella. Nature Microbiology 2023, 8: 1880-1895. PMID: 37640963, PMCID: PMC10962312, DOI: 10.1038/s41564-023-01459-y.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsHumansLeucine-Rich Repeat Serine-Threonine Protein Kinase-2MiceParkinson DiseaseSalmonellaSalmonella InfectionsConceptsLeucine-rich repeat kinase 2Loss of LRRK2Host defense mechanismsKinase leucine-rich repeat kinase 2Parkinson's disease-associated leucine-rich repeat kinase 2Host defense pathwaysBacterial pathogen SalmonellaRepeat kinase 2Salmonella infectionSalmonella-containing vacuolesCell-intrinsic defenseIntracellular pathogensIntracellular SalmonellaFirst lineSalmonella replicationSalmonella mutantsKinase 2Pathogen SalmonellaDefense mechanismsSalmonellaHost mitochondriaDefense pathwaysDeliveryDefense responsesCells
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 roleRole of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis
Lara-Tejero M, Sutterwala FS, Ogura Y, Grant EP, Bertin J, Coyle AJ, Flavell RA, Galán J. Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis. Journal Of Experimental Medicine 2006, 203: 1407-1412. PMID: 16717117, PMCID: PMC2118315, DOI: 10.1084/jem.20060206.Peer-Reviewed Original Research
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, 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.
1996
A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurlum
Kaniga K, Uralil J, Bliska J, Galán J. A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurlum. Molecular Microbiology 1996, 21: 633-641. PMID: 8866485, DOI: 10.1111/j.1365-2958.1996.tb02571.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceCell LineChromosomes, BacterialDisease Models, AnimalDNA, BacterialEpithelial CellsFemaleHumansMacrophagesMiceMice, Inbred BALB CMolecular Sequence DataProtein Tyrosine PhosphatasesSalmonella InfectionsSalmonella typhimuriumSequence Homology, Amino AcidVirulenceConceptsProtein tyrosine phosphataseTyrosine phosphataseEffector proteinsCatalytic domainHost cell signal transduction pathwaysBacterial pathogen Salmonella typhimuriumSignal transduction pathwaysCritical Cys residuesAmino-terminal regionCarboxy-terminal regionPathogen Salmonella typhimuriumCell regulatory moleculesSequence similarityEffector domainSignaling functionsExport proteinCys residuesRegulatory moleculesExoenzyme SSequence analysisPeptide substratesPhosphatase activityCatalytic mechanismProteinYersinia spp
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 calcium