2017
Molecular basis of tactile specialization in the duck bill
Schneider ER, Anderson EO, Mastrotto M, Matson JD, Schulz VP, Gallagher PG, LaMotte RH, Gracheva EO, Bagriantsev SN. Molecular basis of tactile specialization in the duck bill. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 13036-13041. PMID: 29109250, PMCID: PMC5724259, DOI: 10.1073/pnas.1708793114.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAvian ProteinsBeakChickensCloning, MolecularDucksEmbryo, NonmammalianGene ExpressionGenetic VectorsHEK293 CellsHumansIon ChannelsKineticsMechanoreceptorsMechanotransduction, CellularMicePatch-Clamp TechniquesRecombinant ProteinsRNA, Small InterferingSequence Homology, Amino AcidSpecies SpecificityTouchTouch PerceptionTrigeminal GanglionConceptsMolecular basisHeterologous expression systemSpecialist birdsMouse orthologPiezo2 ion channelsTactile specializationExpression systemDuck billMolecular characterizationIon channelsFeeding behaviorEdible matterPiezo2BirdsElectrophysiological characterizationSlow inactivation kineticsOrthologsVertebratesMechanoMechanotransductionKnockdownInactivation kineticsMurky watersHigh densityNeurons
2015
Mutations in the Gardos channel (KCNN4) are associated with hereditary xerocytosis
Glogowska E, Lezon-Geyda K, Maksimova Y, Schulz VP, Gallagher PG. Mutations in the Gardos channel (KCNN4) are associated with hereditary xerocytosis. Blood 2015, 126: 1281-1284. PMID: 26198474, PMCID: PMC4566808, DOI: 10.1182/blood-2015-07-657957.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnemia, Hemolytic, CongenitalBase SequenceDNA Mutational AnalysisExomeFemaleGenes, DominantGenetic Association StudiesHeterozygoteHumansHydrops FetalisIntermediate-Conductance Calcium-Activated Potassium ChannelsIon ChannelsMaleMolecular Sequence DataMutation, MissensePedigreeSequence Homology, Amino AcidConceptsErythrocyte volume homeostasisAutosomal dominant hemolytic anemiaPotassium channel proteinHereditary xerocytosisHeterozygous mutationsChannel proteinsWhole-exome sequencingKCNN4 geneSame residuesSegregation analysisDisease phenotypeMutationsCellular dehydrationChannel mutationsGardos channelHX patientsDifferent mutationsCritical rolePiezo1XerocytosisWater lossVolume homeostasisChannel inactivationRecent studiesDeoxy conditions
2014
Piezo Proteins: Regulators of Mechanosensation and Other Cellular Processes*
Bagriantsev SN, Gracheva EO, Gallagher PG. Piezo Proteins: Regulators of Mechanosensation and Other Cellular Processes*. Journal Of Biological Chemistry 2014, 289: 31673-31681. PMID: 25305018, PMCID: PMC4231648, DOI: 10.1074/jbc.r114.612697.Peer-Reviewed Original ResearchConceptsPiezo proteinsCellular processesMammalian cellsCellular developmentMechanosensory transductionCellular migrationIon channelsHereditary xerocytosisVolume regulationProteinBiologic processesRegulationImportant insightsTransductionMechanosensationRegulatorMutationsXerocytosisProliferationCellsMechanoVariety of disordersElongationMigrationProminent feature
2013
The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation
Harper SL, Sriswasdi S, Tang HY, Gaetani M, Gallagher PG, Speicher DW. The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. Blood 2013, 122: 3045-3053. PMID: 23974198, PMCID: PMC3811177, DOI: 10.1182/blood-2013-02-487702.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCross-Linking ReagentsElliptocytosis, HereditaryErythrocyte MembraneHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSpectrinConceptsHereditary elliptocytosisMembrane destabilizationLarge conformational rearrangementsGel filtration analysisMembrane proteinsTetramer assemblyHereditary pyropoikilocytosisBiophysical analysisCommon hereditary elliptocytosisConformational rearrangementsDimer conformationHelical contentTetramerization siteFiltration analysisSpectrin tetramersNovel mechanismUnknown mechanismMutationsBinding assaysSpectrinChemical crosslinkingErythrocyte shapeTetramerErythrocyte membranesMembrane
2012
Teleost growth factor independence (gfi) genes differentially regulate successive waves of hematopoiesis
Cooney JD, Hildick-Smith GJ, Shafizadeh E, McBride PF, Carroll KJ, Anderson H, Shaw GC, Tamplin OJ, Branco DS, Dalton AJ, Shah DI, Wong C, Gallagher PG, Zon LI, North TE, Paw BH. Teleost growth factor independence (gfi) genes differentially regulate successive waves of hematopoiesis. Developmental Biology 2012, 373: 431-441. PMID: 22960038, PMCID: PMC3532562, DOI: 10.1016/j.ydbio.2012.08.015.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCloning, MolecularConserved SequenceDNA-Binding ProteinsEmbryo, NonmammalianEpistasis, GeneticErythropoiesisEvolution, MolecularGene Expression Regulation, DevelopmentalHematopoiesisHematopoietic Stem CellsHematopoietic SystemModels, BiologicalMolecular Sequence DataZebrafishZebrafish ProteinsConceptsHematopoietic stem cellsTranscription factorsDefinitive hematopoiesisRUNX-1Hematopoietic stem/progenitor cell developmentKey hematopoietic transcription factorsC-MybDefinitive hematopoietic progenitorsHematopoietic transcription factorsProgenitor cell developmentLineage specificationPrimitive hematopoiesisGfi1aaEpistatic relationshipErythroid developmentTranscriptional programsGFI1BHematopoietic lineagesFunctional analysisCritical regulatorCell developmentZebrafishHematopoietic progenitorsDistinct rolesPrimitive progenitorsMutations in the mechanotransduction protein PIEZO1 are associated with hereditary xerocytosis
Zarychanski R, Schulz VP, Houston BL, Maksimova Y, Houston DS, Smith B, Rinehart J, Gallagher PG. Mutations in the mechanotransduction protein PIEZO1 are associated with hereditary xerocytosis. Blood 2012, 120: 1908-1915. PMID: 22529292, PMCID: PMC3448561, DOI: 10.1182/blood-2012-04-422253.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnemia, Hemolytic, CongenitalBase SequenceDNA Mutational AnalysisErythroid CellsExomeFamily HealthFemaleGene ExpressionGenetic Predisposition to DiseaseGenotypeHumansHydrops FetalisIon ChannelsMaleMass SpectrometryMechanotransduction, CellularMolecular Sequence DataMutationPedigreeProteomicsReverse Transcriptase Polymerase Chain ReactionConceptsPiezo proteinsErythrocyte volume homeostasisAutosomal dominant hemolytic anemiaHereditary xerocytosisPiezo familyMammalian cellsTransduction channelsCell mRNADiscovery proteomicsPIEZO1 mutationsGenetic diseasesSegregation analysisDisease phenotypeMutationsLinkage studiesHuman erythrocyte membranesProteinExome sequencingNumber analysisNovel mutationsPiezo1DNA levelsXerocytosisFirst reportVolume homeostasis
2011
Perinatal Onset Mevalonate Kinase Deficiency
Steiner LA, Ehrenkranz RA, Peterec SM, Steiner RD, Reyes-Múgica M, Gallagher PG. Perinatal Onset Mevalonate Kinase Deficiency. Pediatric And Developmental Pathology 2011, 14: 301-306. PMID: 21425920, DOI: 10.2350/11-02-0985-oa.1.Peer-Reviewed Original ResearchConceptsMevalonate kinase deficiencyPeriodic fever syndromeNeonatal periodKinase deficiencyFever syndromeDysmorphic featuresCentral nervous system abnormalitiesIntrauterine viral infectionCholestatic liver diseaseIntrauterine growth restrictionImmediate neonatal periodNervous system abnormalitiesSevere multisystem disorderSepsis syndromeRenal failureCerebral ventriculomegalyLiver diseasePersistent diarrheaClinical findingsPoor prognosisAutopsy findingsGrowth restrictionRare conditionExtramedullary erythropoiesisPerinatal period
2010
A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin [S] *
Li D, Harper SL, Tang HY, Maksimova Y, Gallagher PG, Speicher DW. A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin [S] *. Journal Of Biological Chemistry 2010, 285: 29535-29545. PMID: 20610390, PMCID: PMC2937985, DOI: 10.1074/jbc.m110.145573.Peer-Reviewed Original ResearchConceptsHelix faceRed cell membrane stabilityHomology modelingNon-homologous tailsCell membrane stabilityC-terminal tailWild-type bindingMedium-resolution structureSubtle conformational changesTetramer complexSpectrin tetramer formationChemical Cross-LinkingMembrane skeletonRecombinant domainsTetramer formation
2009
The GPA-dependent, spherostomatocytosis mutant AE1 E758K induces GPA-independent, endogenous cation transport in amphibian oocytes
Stewart AK, Vandorpe DH, Heneghan JF, Chebib F, Stolpe K, Akhavein A, Edelman EJ, Maksimova Y, Gallagher PG, Alper SL. The GPA-dependent, spherostomatocytosis mutant AE1 E758K induces GPA-independent, endogenous cation transport in amphibian oocytes. American Journal Of Physiology - Cell Physiology 2009, 298: c283-c297. PMID: 19907019, PMCID: PMC2822494, DOI: 10.1152/ajpcell.00444.2009.Peer-Reviewed Original Research4,4'-Diisothiocyanostilbene-2,2'-Disulfonic AcidAmbystoma mexicanumAmino Acid SequenceAmphibiansAnemia, Hemolytic, CongenitalAnimalsAnion Exchange Protein 1, ErythrocyteBicarbonatesBumetanideCell MembraneCell Membrane PermeabilityChloridesCloning, MolecularDNA Mutational AnalysisFemaleGlycophorinsHeterozygoteHumansHydrogen-Ion ConcentrationKineticsMaleMembrane PotentialsMiddle AgedMolecular Sequence DataMutation, MissenseOocytesOuabainOxalic AcidRubidium RadioisotopesSeverity of Illness IndexSodium Potassium Chloride Symporter InhibitorsSodium-Potassium-Exchanging ATPaseSulfatesXenopus laevisSites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity
Rinehart J, Maksimova YD, Tanis JE, Stone KL, Hodson CA, Zhang J, Risinger M, Pan W, Wu D, Colangelo CM, Forbush B, Joiner CH, Gulcicek EE, Gallagher PG, Lifton RP. Sites of Regulated Phosphorylation that Control K-Cl Cotransporter Activity. Cell 2009, 138: 525-536. PMID: 19665974, PMCID: PMC2811214, DOI: 10.1016/j.cell.2009.05.031.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsHumansMiceMolecular Sequence DataPhosphorylationSequence AlignmentSymportersConceptsIntrinsic transport activityK-Cl cotransporterTransport activityCell volume regulationRegulated phosphorylationRNA interferenceAlanine substitutionsCultured cellsHomologous sitesKCC activityCl exitWNK1 expressionNeonatal mouse brainVolume regulationNeuronal functionHypotonic conditionsActive cotransportPhosphorylationIntracellular chloride concentrationCotransporter activityKCC3Human red blood cellsKCC2 activationFundamental roleMouse brain
2008
Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site
Gaetani M, Mootien S, Harper S, Gallagher PG, Speicher DW. Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site. Blood 2008, 111: 5712-5720. PMID: 18218854, PMCID: PMC2424163, DOI: 10.1182/blood-2007-11-122457.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnemia, Hemolytic, CongenitalBinding SitesCalorimetry, Differential ScanningCircular DichroismEntropyErythrocytesGene ExpressionGenotypeHumansMolecular Sequence DataPhenotypePoint MutationProtein BindingRecombinant ProteinsSpectrinSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationStructure-Activity Relationship
2001
Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain
Zhang Z, Weed S, Gallagher P, Morrow J. Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain. Blood 2001, 98: 1645-1653. PMID: 11535493, DOI: 10.1182/blood.v98.6.1645.Peer-Reviewed Original ResearchConceptsSelf-association domainPoint mutationsHuman sequenceDrosophila alpha-spectrinDynamic molecular modelingHuman erythrocyte spectrinCytoskeletal functionSpecific point mutationsConservative substitutionsPrimary sequenceConformational rearrangementsAlpha-spectrinHelical regionHydrophilic residuesAmino acidsMutationsSpectrinSalt bridgeErythrocyte spectrinStructural consequencesPathogenic mutationsRepeat unitsMolecular modelingSequenceStructural disruption
2000
Genomic organization and chromosomal localization of the murine 2 P domain potassium channel gene Kcnk8: conservation of gene structure in 2 P domain potassium channels
Bockenhauer D, Nimmakayalu M, Ward D, Goldstein S, Gallagher P. Genomic organization and chromosomal localization of the murine 2 P domain potassium channel gene Kcnk8: conservation of gene structure in 2 P domain potassium channels. Gene 2000, 261: 365-372. PMID: 11167025, DOI: 10.1016/s0378-1119(00)00492-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChromosome MappingDNADNA, ComplementaryElectrophysiologyExonsGenesIn Situ Hybridization, FluorescenceIntronsMiceMolecular Sequence DataOocytesPhylogenyPotassium ChannelsPotassium Channels, Tandem Pore DomainProtein Structure, TertiaryRNA, ComplementarySequence Analysis, DNAXenopus laevisConceptsPotassium channel genesDomain potassium channelsChromosomal localizationGene structureOocyte expression systemCDNA sequenceXenopus laevis oocyte expression systemExpression systemChannel genesPotential transmembrane helicesIntron/exon boundariesSingle EF-hand motifOpen reading framePotassium channelsEF-hand motifsEvolutionary conservationGenomic organizationCellular chaperonesGenomic structureComposite cDNAPotential SH3Transmembrane helicesGenome databaseChromosomal genesReading frameProton Block and Voltage Gating Are Potassium-dependent in the Cardiac Leak Channel Kcnk3*
Lopes C, Gallagher P, Buck M, Butler M, Goldstein S. Proton Block and Voltage Gating Are Potassium-dependent in the Cardiac Leak Channel Kcnk3*. Journal Of Biological Chemistry 2000, 275: 16969-16978. PMID: 10748056, DOI: 10.1074/jbc.m001948200.Peer-Reviewed Original ResearchConceptsExternal potassium levelsGenomic structureUnique functional attributesProton blockIndependent molecular entitiesP domainMurine examplesFunctional attributesBiophysical propertiesPhysiological voltage rangePhysiological levelsPotassium channelsLeak conductanceMolecular entitiesSubunitsPotassium leak conductanceKCNK3Conductance
1998
An Alternate Promoter Directs Expression of a Truncated, Muscle-specific Isoform of the Human Ankyrin 1 Gene*
Gallagher P, Forget B. An Alternate Promoter Directs Expression of a Truncated, Muscle-specific Isoform of the Human Ankyrin 1 Gene*. Journal Of Biological Chemistry 1998, 273: 1339-1348. PMID: 9430667, DOI: 10.1074/jbc.273.3.1339.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnkyrinsBase SequenceCloning, MolecularDNA, ComplementaryErythroid Precursor CellsExonsGene Expression RegulationHumansMolecular Sequence DataMuscle, SkeletalMusclesMyocardiumMyoD ProteinPromoter Regions, GeneticRecombinant ProteinsTranscriptional ActivationConceptsKilobase pairsMuscle cDNADeduced amino acid sequenceCorresponding chromosomal geneHydrophobic NH2 terminusCultured C2C12 muscle cellsHuman ankyrin-1 geneSkeletal muscle cDNADNA-protein interactionsE-box consensusAmino acid sequenceK562 cellsMuscle-specific isoformPromoter directs expressionC2C12 muscle cellsAnkyrin-1 geneReporter gene plasmidHigh-level expressionNorthern blot analysisErythroid genesErythrocyte membrane proteinsSingle Sp1Erythroid promoterAlternative splicingRich promoter
1997
Structure and Organization of the Human Ankyrin-1 Gene BASIS FOR COMPLEXITY OF PRE-mRNA PROCESSING*
Gallagher P, Tse W, Scarpa A, Lux S, Forget B. Structure and Organization of the Human Ankyrin-1 Gene BASIS FOR COMPLEXITY OF PRE-mRNA PROCESSING*. Journal Of Biological Chemistry 1997, 272: 19220-19228. PMID: 9235914, DOI: 10.1074/jbc.272.31.19220.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnkyrinsBase SequenceBrainCloning, MolecularExonsHumansIntronsMolecular Sequence DataPoly ARNA PrecursorsConceptsGenomic structureANK-1 geneSpectrin-binding domainMembrane-binding domainIntron/exon boundariesAlternative polyadenylation signalsPre-mRNA processingBrain-specific transcriptFurther genetic studiesErythrocyte membrane proteinsErythroid transcriptsCommon hemolytic anemiaGene basisAlternative splicingRegulatory domainProtein domainsChromosomal genesMembrane proteinsKilobase pairsPolyadenylation signalMembrane skeletonPlasma membraneExon boundariesGenetic studiesAnkyrin 1
1996
Molecular basis and haplotyping of the alphaII domain polymorphisms of spectrin: application to the study of hereditary elliptocytosis and pyropoikilocytosis.
Gallagher PG, Kotula L, Wang Y, Marchesi SL, Curtis PJ, Speicher DW, Forget BG. Molecular basis and haplotyping of the alphaII domain polymorphisms of spectrin: application to the study of hereditary elliptocytosis and pyropoikilocytosis. American Journal Of Human Genetics 1996, 59: 351-9. PMID: 8755921, PMCID: PMC1914747.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnemia, Hemolytic, CongenitalAsianAsian PeopleBase SequenceBiological EvolutionBlack PeopleElliptocytosis, HereditaryErythrocytes, AbnormalHaplotypesHumansModels, GeneticMolecular Sequence DataMutagenesis, InsertionalPolymorphism, GeneticPrevalenceRepetitive Sequences, Nucleic AcidSpectrinUnited StatesWhite PeopleConceptsAlpha-spectrin geneAmino acid sequenceAcid sequenceHereditary elliptocytosisAlpha-spectrin chainHereditary pyropoikilocytosisPrincipal structural proteinErythrocyte membrane skeletonSingle nucleotide substitutionEvolutionary originLimited tryptic digestionMembrane skeletonMolecular basisGenomic DNANucleotide substitutionsStructural proteinsAlpha-spectrinDifferent haplotypesFounder effectGenesLinkage disequilibriumOnly haplotypeSpectrin proteinsCommon haplotypeTryptic digestionThe lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle.
Weed SA, Stabach PR, Oyer CE, Gallagher PG, Morrow JS. The lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle. Laboratory Investigation 1996, 74: 1117-29. PMID: 8667615.Peer-Reviewed Original ResearchConceptsBeta ISpectrin skeletonSkeletal muscleMost such mutationsGene transferAdult mouse skeletal muscleDominant-negative fashionErythroid lineage cellsNeonatal skeletal muscleCultured muscle cellsAlpha beta heterodimersErythrocyte shape abnormalitiesMuscle cellsMouse skeletal muscleDefective proteinSpectrin geneAlternative transcriptsHemolytic phenotypeCDNA constructsNull phenotypeC2C12 myoblastsBeta heterodimerSpectrin mutationsSedimentation velocity analysisIntracellular distributionGenomic Organization and 5′-Flanking DNA Sequence of the Murine Stomatin Gene (Epb72)
Gallagher P, Turetsky T, Mentzer W. Genomic Organization and 5′-Flanking DNA Sequence of the Murine Stomatin Gene (Epb72). Genomics 1996, 34: 410-412. PMID: 8786142, DOI: 10.1006/geno.1996.0304.Peer-Reviewed Original ResearchConceptsStomatin geneDNA sequencesPotential DNA-binding proteinsIntegral membrane proteinsDNA-binding proteinsGenomic DNA sequencesHousekeeping gene promoterGenomic organizationExon structureGenomic structureChromosomal genesMembrane proteinsGene promoterConsensus sequenceGenomic DNAProtein structureGenesHereditary stomatocytosisSequenceProteinErythrocyte membranesStomatinCloningExonsPromoter
1995
Structure, Organization, and Expression of the Human Band 7.2b Gene, a Candidate Gene for Hereditary Hydrocytosis (∗)
Gallagher P, Forget B. Structure, Organization, and Expression of the Human Band 7.2b Gene, a Candidate Gene for Hereditary Hydrocytosis (∗). Journal Of Biological Chemistry 1995, 270: 26358-26363. PMID: 7592848, DOI: 10.1074/jbc.270.44.26358.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnemia, HemolyticAnimalsBase SequenceBlood ProteinsBlotting, NorthernCell LineConsensus SequenceDNA PrimersDNA, ComplementaryExonsGene ExpressionGenetic VariationHominidaeHumansIntronsLeukemia, Erythroblastic, AcuteMembrane ProteinsMiceMolecular Sequence DataPolymerase Chain ReactionPolymorphism, GeneticPromoter Regions, GeneticRecombinant Fusion ProteinsRegulatory Sequences, Nucleic AcidRestriction MappingRNA, MessengerTransfectionTumor Cells, CulturedConceptsSingle transcription initiation siteSimple sequence repeat polymorphismKilobases of DNATranscription initiation siteAlternative polyadenylation signalsFurther genetic studiesHigh-level expressionNorthern blot analysisPattern of expressionWide tissue distributionGenomic structureRich promoterNonerythroid cellsChromosomal genesPolyadenylation signalMembrane skeletonGene cDNAGene promoterReporter geneCandidate genesRecognition sequenceGenetic studiesInitiation siteGenesBase pairs