2021
Composition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System
Tachiyama S, Skaar R, Chang Y, Carroll BL, Muthuramalingam M, Whittier SK, Barta ML, Picking WL, Liu J, Picking WD. Composition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System. Frontiers In Cellular And Infection Microbiology 2021, 11: 682635. PMID: 34150677, PMCID: PMC8211105, DOI: 10.3389/fcimb.2021.682635.Peer-Reviewed Original ResearchConceptsType III secretion systemCytoplasmic sorting platformSorting platformSecretion systemTwo-hybrid analysisCryo-electron tomography dataC-terminal domainShigella type III secretion systemFull-length copiesBiophysical propertiesDistinct biophysical propertiesSpa47 ATPaseT3SS injectisomeEffector proteinsSecretion substratesDistinct complexesIntracellular nicheBasal bodiesPrimary virulence factorSpa33Host cellsHeterotrimerPrecise makeupVirulence factorsMxiK
2020
The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform
Muthuramalingam M, Whittier SK, Lovell S, Battaile KP, Tachiyama S, Johnson DK, Picking WL, Picking WD. The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform. Journal Of Molecular Biology 2020, 432: 166693. PMID: 33122003, PMCID: PMC10550303, DOI: 10.1016/j.jmb.2020.10.027.Peer-Reviewed Original ResearchConceptsInner membrane ringBasal bodiesCytoplasmic domainSorting platformFirst high-resolution structureType III secretion systemCytoplasmic sorting platformTwo-hybrid analysisGram-negative bacterial pathogensProtein family membersNormal cellular functionHigh-resolution structuresAtomic resolution modelsHelix-rich structureEukaryotic cellsT3SS apparatusAdaptor proteinCellular functionsSecretion systemMembrane ringMechanistic interfaceTip complexExternal needleRadial spokesProtein
2014
Discovering the pre‐60S ribosome biogenesis factor interactome (560.7)
McCann K, Charette J, Vincent N, Baserga S. Discovering the pre‐60S ribosome biogenesis factor interactome (560.7). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.560.7.Peer-Reviewed Original ResearchRibosome assemblyGlycerol gradient sedimentation analysisTwo-hybrid analysisHigh-throughput yeastHigh-confidence interactionsPotential regulatory mechanismsGradient sedimentation analysisRNA helicasesBiogenesis factorsSmaller subcomplexesMDa complexNucleolar proteinsRibosomal subunitRegulatory mechanismsDifferent proteinsSubcomplexHelicasesGlycerol gradientsIndependent validation experimentsInteractomeSedimentation analysisYeastCurrent knowledgeProteinAssembly
2013
NOL11, implicated in the pathogenesis of North American Indian Childhood Cirrhosis, is required for pre‐rRNA transcription and processing
Baserga S, Freed E, Prieto J, McCann K, McStay B. NOL11, implicated in the pathogenesis of North American Indian Childhood Cirrhosis, is required for pre‐rRNA transcription and processing. The FASEB Journal 2013, 27: 552.1-552.1. DOI: 10.1096/fasebj.27.1_supplement.552.1.Peer-Reviewed Original ResearchNorth American Indian childhood cirrhosisRibosome biogenesisSmall subunitC-terminusInteraction partnersDefective protein-protein interactionsTwo-hybrid cDNA libraryUncharacterized nucleolar proteinRibosome biogenesis factorsRibosome biogenesis defectsTwo-hybrid analysisPre-rRNA transcriptionRibosomal small subunitProtein-protein interactionsCo-immunoprecipitation experimentsRDNA transcriptionBiogenesis defectsBiogenesis factorsNucleolar proteinsNovel proteinCDNA libraryCirhinAffinity purificationDisease mutationsSiRNA knockdown
2011
Interaction of Recombinant Myocilin with the Matricellular Protein SPARC: Functional Implications
Aroca-Aguilar JD, Sánchez-Sánchez F, Ghosh S, Fernández-Navarro A, Coca-Prados M, Escribano J. Interaction of Recombinant Myocilin with the Matricellular Protein SPARC: Functional Implications. Investigative Ophthalmology & Visual Science 2011, 52: 179-189. PMID: 20926826, PMCID: PMC3053273, DOI: 10.1167/iovs.09-4866.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBlotting, WesternCalcium-Binding ProteinsCell LineChromatography, High Pressure LiquidCytoskeletal ProteinsExtracellular Matrix ProteinsEye ProteinsGene Expression ProfilingGlycoproteinsHumansKidneyMicroscopy, FluorescenceMolecular Sequence DataOsteonectinPolymerase Chain ReactionProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsTwo-Hybrid System TechniquesConceptsHEK 293T cellsSolid-phase binding assaysInteraction of myocilinRecombinant proteinsRecombinant myocilinMatricellular proteinEC domainTerminal olfactomedin domainTwo-hybrid analysisTwo-hybrid systemProtein-protein interactionsFull-length myocilinC-terminal domainN-terminal domainC-terminal regionCalcium binding domainsBinding assaysOlfactomedin domainC-terminal fragmentBinding domainsLinker regionUnknown functionExtracellular glycoproteinIntracellular interactionsSPARC family
2000
Cellular Mechanisms Regulating Protein Phosphatase-1 A KEY FUNCTIONAL INTERACTION BETWEEN INHIBITOR-2 AND THE TYPE 1 PROTEIN PHOSPHATASE CATALYTIC SUBUNIT*
Frederick D, Huang H, Yang J, Helps N, Cohen P, Nairn A, DePaoli-Roach A, Tatchell K, Connor J, Shenolikar S. Cellular Mechanisms Regulating Protein Phosphatase-1 A KEY FUNCTIONAL INTERACTION BETWEEN INHIBITOR-2 AND THE TYPE 1 PROTEIN PHOSPHATASE CATALYTIC SUBUNIT*. Journal Of Biological Chemistry 2000, 275: 18670-18675. PMID: 10748125, DOI: 10.1074/jbc.m909312199.Peer-Reviewed Original ResearchConceptsPP1 catalytic subunitCatalytic subunitType 1 protein phosphatase catalytic subunitAmino acidsProtein phosphatase catalytic subunitN-terminusProtein serine/threonineN-terminal 35 amino acidsInhibitor 2Phosphatase catalytic subunitTwo-hybrid analysisNovel regulatory interactionsProtein phosphatase 1Serine/threoninePull-down assaysSite-directed mutagenesisN-terminal sequencePP1 mutantsKey functional interactionsPP1 inhibitorPP1 enzymesPP1 inhibitionPhosphatase 1Regulatory interactionsSaccharomyces cerevisiae
1999
Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat
Shugrue C, Kolen E, Peters H, Czernik A, Kaiser C, Matovcik L, Hubbard A, Gorelick F. Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat. Journal Of Cell Science 1999, 112: 4547-4556. PMID: 10574704, PMCID: PMC5567750, DOI: 10.1242/jcs.112.24.4547.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell LineCloning, MolecularCOP-Coated VesiclesDNA, ComplementaryFungal ProteinsGTPase-Activating ProteinsHumansMembrane ProteinsMolecular Sequence DataNuclear Pore Complex ProteinsPhosphoproteinsRatsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidVesicular Transport ProteinsConceptsMammalian orthologuesCOPII coatSequential column chromatographyTwo-hybrid analysisIntracellular vesicular traffickingSmall punctate structuresVesicle-associated proteinLiver cDNA libraryCultured cell linesRat liver cDNA libraryVesicular buddingVesicular traffickingNovel proteinSignificant homologyTarget membraneCDNA libraryPunctate structuresSec13pSec31pIntact cellsP137ProteinOrthologuesCell linesColumn chromatography
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