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 ResearchConceptsLeucine-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
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
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
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 cellsRacRearrangementCellsTransduction
2000
Biophysical characterization of SipA, an actin‐binding protein from Salmonella enterica
Mitra K, Zhou D, Galán J. Biophysical characterization of SipA, an actin‐binding protein from Salmonella enterica. FEBS Letters 2000, 482: 81-84. PMID: 11018527, DOI: 10.1016/s0014-5793(00)02040-8.Peer-Reviewed Original ResearchConceptsActin dynamicsCoiled-coil domainF-actin stabilityActin-binding proteinsActin cytoskeleton reorganizationNon-phagocytic cellsBacterial entryCytoskeleton reorganizationAdjacent actin monomersC-terminal fragmentBiophysical characterizationF-actinCellular responsesHost cellsBacterial uptakeActin monomersProteinSalmonella entericaHelical conformationSalmonella enterica infectionsIntestinal epitheliumEnterica infectionsEssential stepSIPACellsDevelopmental Control of Endocytosis in Dendritic Cells by Cdc42
Garrett W, Chen L, Kroschewski R, Ebersold M, Turley S, Trombetta S, Galán J, Mellman I. Developmental Control of Endocytosis in Dendritic Cells by Cdc42. Cell 2000, 102: 325-334. PMID: 10975523, DOI: 10.1016/s0092-8674(00)00038-6.Peer-Reviewed Original Research
1999
Type III Secretion Machines: Bacterial Devices for Protein Delivery into Host Cells
Galán J, Collmer A. Type III Secretion Machines: Bacterial Devices for Protein Delivery into Host Cells. Science 1999, 284: 1322-1328. PMID: 10334981, DOI: 10.1126/science.284.5418.1322.Peer-Reviewed Original ResearchConceptsSecretion systemComplex protein secretion systemsHost cellsType III secretion systemBacterial effector proteinsProtein secretion systemAnimal pathogenic bacteriaHost cellular functionsGram-negative pathogenic bacteriaBacterial devicesPathogenic bacteriaEffector proteinsCellular functionsFlagellar apparatusBacterial speciesEffector moleculesProtein deliveryBacteriaCellsNovel preventionBiologySpeciesPlantsProteinTherapeutic approaches
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 stimulationProteinCellsThe 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
1997
The invasion-associated type-III protein secretion system inSalmonella – a review1Presented at the Workshop on `Type-4 Pili – Biogenesis, Adhesins, Protein Export, and DNA Import', Schloss Ringberg, Germany, 26–29 November 1995.1
Collazo C, Galán J. The invasion-associated type-III protein secretion system inSalmonella – a review1Presented at the Workshop on `Type-4 Pili – Biogenesis, Adhesins, Protein Export, and DNA Import', Schloss Ringberg, Germany, 26–29 November 1995.1. Gene 1997, 192: 51-59. PMID: 9224874, DOI: 10.1016/s0378-1119(96)00825-6.Peer-Reviewed Original ResearchConceptsProtein secretion systemSecretion systemType-4 Pili – BiogenesisHost cellsEukaryotic host cellsSpecialized protein secretion systemNon-phagocytic cellsMolecular genetic analysisDNA importPili biogenesisProtein exportSchloss RingbergCentisome 63Bacterial chromosomeAnimal pathogensGenetic analysisPathogenicity islandGenetic determinantsCellsReview1PresentedChromosomesPlantsProteinTranslocationAdhesins
1996
CROSS-TALK BETWEEN BACTERIAL PATHOGENS AND THEIR HOST CELLS
Galán J, Bliska J. CROSS-TALK BETWEEN BACTERIAL PATHOGENS AND THEIR HOST CELLS. Annual Review Of Cell And Developmental Biology 1996, 12: 221-255. PMID: 8970727, DOI: 10.1146/annurev.cellbio.12.1.221.Peer-Reviewed Original ResearchConceptsHost cellsHost cell signal transduction pathwaysProtein secretion systemHost cellular functionsSpecialized protein secretion systemSignal transduction pathwaysBacterial pathogensHost cell interactionsSecretion systemTransduction pathwaysBacterial proteinsCell physiologyBiochemical interactionsDiverse groupPathogensNovel therapeutic approachesCellsProteinTranslocationBetter understandingInteractionPathwayPhysiologyTherapeutic approachesBasic aspectsMolecular 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 progressHomologyLociOrganismsProtein
1994
Interactions of bacteria with non-phagocytic cells
Galan J. Interactions of bacteria with non-phagocytic cells. Current Opinion In Immunology 1994, 6: 590-595. PMID: 7946047, DOI: 10.1016/0952-7915(94)90146-5.Peer-Reviewed Original ResearchThe 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 sizeCellsMembersHomologuesSalmonella entry into mammalian cells: different yet converging signal transduction pathways?
Galán J. Salmonella entry into mammalian cells: different yet converging signal transduction pathways? Trends In Cell Biology 1994, 4: 196-199. PMID: 14731677, DOI: 10.1016/0962-8924(94)90136-8.Peer-Reviewed Original ResearchSignal transduction pathwaysTransduction pathwaysHost cell signal transduction pathwaysCell signal transduction pathwaysDifferent signaling pathwaysCommon effector moleculesMammalian cellsSalmonella entryDifferent cell linesSignaling pathwaysDiverse pathwaysEffector moleculesCell linesPathwayCommon mechanismBacteriaSalmonella bacteriaCellsUptakeContact 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 calcium