2022
Assembly and architecture of the type III secretion sorting platform
Soto J, Galán J, Lara-Tejero M. Assembly and architecture of the type III secretion sorting platform. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2218010119. PMID: 36512499, PMCID: PMC9907115, DOI: 10.1073/pnas.2218010119.Peer-Reviewed Original ResearchConceptsType III secretion machinesType III secretion systemTarget eukaryotic cellsType III secretionSecretion of proteinsBacterial nanomachinesSecretion machineEukaryotic cellsExport pathwayImportant bacterial pathogensSecretion systemBacterial structureAntivirulence strategiesCoordinated mechanismFunctional complexityBacterial pathogensGenetic deletionStructure modelingProtein deliveryAssemblyRational developmentCross-linking strategyAssembly processProteinDeletion
2001
SALMONELLA INTERACTIONS WITH HOST CELLS: Type III Secretion at Work
Galán J. SALMONELLA INTERACTIONS WITH HOST CELLS: Type III Secretion at Work. Annual Review Of Cell And Developmental Biology 2001, 17: 53-86. PMID: 11687484, DOI: 10.1146/annurev.cellbio.17.1.53.Peer-Reviewed Original ResearchConceptsBacterial proteinsBacterial pathogen Salmonella entericaHost cellsType III secretion systemActin cytoskeleton dynamicsType III secretionHost cell functionsPathogen Salmonella entericaMolecular tinkeringConvergent evolutionEndocytic traffickingCytoskeleton dynamicsSpecialized organellesCellular functionsSecretion systemMicrobial pathogenesisRemarkable pathogenHost proteinsSalmonella interactionsVertebrate hostsProteinRemarkable arrayCoordinated actionCell functionSalmonella entericaMaintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
Stebbins C, Galán J. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 2001, 414: 77-81. PMID: 11689946, DOI: 10.1038/35102073.Peer-Reviewed Original ResearchConceptsEffector proteinsSecretion systemType III protein secretion systemBacterial type III secretionSpecific cytosolic chaperonesSuch effector proteinsType III secretion systemSecretion-competent stateVirulence effector proteinsProtein secretion systemChaperone-binding domainHost cell cytosolType III secretionType III apparatusCytosolic chaperonesUnfolded polypeptidesSecretion machineryCognate chaperoneÅ resolutionChaperonesCell cytosolChaperone moleculesEffective translocationBacterial pathogensHydrophobic interface
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