2007
Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis
Krendel M, Osterweil EK, Mooseker MS. Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis. FEBS Letters 2007, 581: 644-650. PMID: 17257598, PMCID: PMC1861834, DOI: 10.1016/j.febslet.2007.01.021.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsDynaminsEndocytosisHeLa CellsHumansImmunoprecipitationMiceMyosin Type INerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingProtein TransportRatsSrc Homology DomainsSynapsesTissue ExtractsTransferrinTwo-Hybrid System TechniquesConceptsSH3 domainMyosin 1eSynaptojanin 1Myosin IIntact SH3 domainDominant-negative mannerReceptor-mediated endocytosisHigher eukaryotesArp2/3 complexInhibits endocytosisPlasma membraneActin polymerizationImportant regulatorEndocytosisHuman class IProminent functionDynaminTail regionDomainEukaryotesClathrinYeastRegulatorProteinBinds
2005
Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae
Shih J, Reck-Peterson S, Newitt R, Mooseker M, Aebersold R, Herskowitz I. Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae. Molecular Biology Of The Cell 2005, 16: 4595-4608. PMID: 16030260, PMCID: PMC1237067, DOI: 10.1091/mbc.e05-02-0108.Peer-Reviewed Original ResearchConceptsCell polarityPolarity proteinsActin functionCell wall morphogenesisCell polarity proteinsYeast cell polarityPresumptive bud siteCell separation defectATP-sensitive mannerTandem mass spectrometry analysisNonessential proteinsWall morphogenesisMolecular functionsBud sitePolarized localizationSpa2pMass spectrometry analysisSite of growthSaccharomyces cerevisiaeMyo2pCoimmunoprecipitation strategyCell cycleF-actinIndirect interactionsProteinMyosin-1a Is Critical for Normal Brush Border Structure and Composition
Tyska M, Mackey A, Huang J, Copeland N, Jenkins N, Mooseker M. Myosin-1a Is Critical for Normal Brush Border Structure and Composition. Molecular Biology Of The Cell 2005, 16: 2443-2457. PMID: 15758024, PMCID: PMC1087248, DOI: 10.1091/mbc.e04-12-1116.Peer-Reviewed Original ResearchConceptsMyosin-1aWhole animal phenotypesWhole animal levelIntermediate filament proteinsEctopic recruitmentFunctional redundancyAnimal phenotypesBrush borderMyosin 1cOvert phenotypeBrush border structureFilament proteinsMembrane componentsCellular levelVertebrate myosinsPhenotypeSigns of stressAnimal levelKnockout miceSignificant perturbationsEnterocytesMultifunctional componentsGenesDistinct changesProtein
2000
The mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a
Jones J, Huang J, Mermall V, Hamilton B, Mooseker M, Escayg A, Copeland N, Jenkins N, Meisler M. The mouse neurological mutant flailer expresses a novel hybrid gene derived by exon shuffling between Gnb5 and Myo5a. Human Molecular Genetics 2000, 9: 821-828. PMID: 10749990, DOI: 10.1093/hmg/9.5.821.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainDNA, ComplementaryExonsFungal ProteinsGene DosageGenes, RecessiveGTP-Binding Protein beta SubunitsIntronsMiceMice, Inbred C57BLMice, Mutant StrainsMicroscopy, ElectronMolecular Sequence DataMonomeric GTP-Binding ProteinsMyosin Type IMyosinsPurkinje CellsRNA, MessengerSaccharomyces cerevisiae ProteinsConceptsN-terminal 83 amino acidsAmino acidsWild-type proteinGlobular tail domainNon-homologous recombinationSmooth endoplasmic reticulum vesiclesNovel hybrid geneDominant-negative mechanismExon shufflingChromosomal arrangementsMammalian mutationsNew genesNovel genesUnrelated genesEndoplasmic reticulum vesiclesTail domainHybrid geneMutational mechanismsTerminal exonIntracellular transportGenetic studiesGenesExonsProteinGNB5
1999
An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contact
1998
Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport
Evans L, Lee A, Bridgman P, Mooseker M. Vesicle-associated brain myosin-V can be activated to catalyze actin-based transport. Journal Of Cell Science 1998, 111: 2055-2066. PMID: 9645952, DOI: 10.1242/jcs.111.14.2055.Peer-Reviewed Original ResearchConceptsMyosin VVesicle proteinsTotal vesicle proteinSynaptic vesicle proteinsInitial fractionation stepSynaptic vesicle marker proteinActin transportBrain myosin-VOrganelle transportActin filament motilityOrganelle motorFunctional analysisVesicle fractionFunction-blocking antibodiesLocalization studiesMarker proteinsImmunoelectron microscopyMotility assaysMotor domainProteinVesiclesFilament motilityVesicle integrityActinVesicle surface
1997
Effects of shaker‐1 mutations on myosin‐VIIa protein and mRNA expression
Hasson T, Walsh J, Cable J, Mooseker M, Brown S, Steel K. Effects of shaker‐1 mutations on myosin‐VIIa protein and mRNA expression. Cytoskeleton 1997, 37: 127-138. PMID: 9186010, DOI: 10.1002/(sici)1097-0169(1997)37:2<127::aid-cm5>3.0.co;2-5.Peer-Reviewed Original ResearchConceptsShaker-1 mutationsWild-type levelsNorthern blot analysisMammalian diseasesActin cytoskeletonMyosin VIIaShaker-1 miceGene expressionUnconventional myosinMRNA expressionProteinMyosin-VIIa mutationsImmunoblot analysisMotor domainRange of expressionMutationsBlot analysisAllelesProtein expressionTissue functionExpressionLife spanSH1Inner earLight microscopic level
1996
The actin-related proteins
Frankel S, Mooseker M. The actin-related proteins. Current Opinion In Cell Biology 1996, 8: 30-37. PMID: 8791406, DOI: 10.1016/s0955-0674(96)80045-7.Peer-Reviewed Original ResearchConceptsActin-related proteinsHsp/Hsc70Family of proteinsClear sequence homologyPrimary structural dataCell cycle proteinsStructural dataFunctional diversitySugar kinasesSequence homologyActin filamentsCycle proteinsFunctional contextProteinActinBiochemical analysisChromatinHsc70FamilyHomologyKinaseStructural elementsMicrotubulesMembersDiversity
1994
Identification of a Divergent Actin-related Protein in Drosophila
Frankel S, Heintzelman M, Artavanis-Tsakonas S, Mooseker M. Identification of a Divergent Actin-related Protein in Drosophila. Journal Of Molecular Biology 1994, 235: 1351-1356. PMID: 8308899, DOI: 10.1006/jmbi.1994.1090.Peer-Reviewed Original ResearchConceptsActin-related proteinsAmino acid identityPrimary sequence homologyDivergent actinConventional actinPolytene chromosomesEarly embryogenesisAcid identityX chromosomeSequence homologyGenomic DNAOverall divergenceSequence insertionNew isotypeActinDrosophilaProteinEmbryogenesisChromosomesHomologyGenesStages of developmentTranscriptsUnique locationLater stages
1992
Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation.
Schafer D, Mooseker M, Cooper J. Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation. Journal Of Cell Biology 1992, 118: 335-346. PMID: 1629237, PMCID: PMC2290044, DOI: 10.1083/jcb.118.2.335.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsActinsAnimalsAntibodiesCells, CulturedChick EmbryoChickensCochleaDestrinElectrophoresis, Polyacrylamide GelEpithelial CellsEpitheliumFluorescent Antibody TechniqueIntestinesKidneyMacromolecular SubstancesMicrofilament ProteinsMicrovilliMusclesPigment Epithelium of EyeSubcellular FractionsConceptsIntestinal epithelial cellsNuclei of cellsBiochemical fractionationJunctional complexesActin filamentsCell-cell junctional complexesSingle intestinal epithelial cellsBarbed endsEpithelial cellsSensory epitheliumCell-cell contactIntact intestinal epithelial cellsAffinity-purified polyclonal antibodiesProtein bindsCapping proteinIntestinal epitheliumZonula adherensCell junctionsChick embryo kidney cellsPattern coincidentEmbryo kidney cellsProteinConfocal microscopyKidney cellsIsolated intestinal epithelial cells
1989
ZO-1 and cingulin: tight junction proteins with distinct identities and localizations
Stevenson B, Heintzelman M, Anderson J, Citi S, Mooseker M. ZO-1 and cingulin: tight junction proteins with distinct identities and localizations. American Journal Of Physiology 1989, 257: c621-c628. PMID: 2679124, DOI: 10.1152/ajpcell.1989.257.4.c621.Peer-Reviewed Original ResearchConceptsCell-cell contactPlasma membraneHepatoma tissue cultureZO-1MDCK cellsMadin-Darby canine kidney cellsCanine kidney cellsSubconfluent MDCK cellsSingle polypeptideCingulinHepatoma cell lineMolecular massChicken small intestineDistinct localizationImmunoblot analysisJunctional membranesImmunofluorescent localizationCell linesKidney cellsJunction proteinsKidney distalTight junctionsChicken intestineConfluent monolayersProteinFunctional diversity among spectrin isoforms
Coleman T, Fishkind D, Mooseker M, Morrow J. Functional diversity among spectrin isoforms. Cytoskeleton 1989, 12: 225-247. PMID: 2655937, DOI: 10.1002/cm.970120405.Peer-Reviewed Original ResearchConceptsSpectrin isoformsBeta subunitMembrane skeletal proteinsFunctional diversityUbiquitous familySubcellular localizationMembrane linkageCommon alpha subunitSkeletal proteinsAlpha subunitNonerythroid spectrinStructural comparisonCell typesMajor functional differencesSpectrinFunctional differencesSubunitsIsoformsFunctional propertiesSummary of studiesProteinDiversityObserved differencesOwn laboratoryLinkage
1988
A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin
Petrucci T, Mooseker M, Morrow J. A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin. Journal Of Cellular Biochemistry 1988, 36: 25-35. PMID: 3125185, DOI: 10.1002/jcb.240360104.Peer-Reviewed Original ResearchConceptsBovine synapsin ISynapsin IActin binding proteinsPeptide mappingTwo-dimensional peptide mapsSmall synaptic vesiclesPhosphorylation controlBundling proteinActin bindingUnrelated proteinsActin bundlesActin filamentsNeuronal phosphoproteinSynapsin I.Binding proteinVivo roleSynaptic vesiclesParent proteinProteinPeptide mapsChymotryptic digestionVillinPeptide fragmentsCross reactFragments
1987
Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border.
Carboni J, Howe C, West A, Barwick K, Mooseker M, Morrow J. Characterization of intestinal brush border cytoskeletal proteins of normal and neoplastic human epithelial cells. A comparison with the avian brush border. American Journal Of Pathology 1987, 129: 589-600. PMID: 3425692, PMCID: PMC1899811.Peer-Reviewed Original ResearchConceptsMicrovillar actin bundlesActin binding proteinsHuman brush borderIntestinal epithelial cell brush bordersEpithelial cell brush bordersBrush borderMicrovillar proteinsHuman epithelial cellsCytoskeletal matrixCytoskeletal proteinsMultiple proteinsActin bundlesImmunolocalization studiesSpectrin isoformsMammalian sourcesMajor proteinsDifferentiation stateBinding proteinProtein myosinProteinTerminal webCell brush borderCytoskeletonNeoplastic stateMature enterocytes
1986
Calcium and the Regulation of Cytoskeletal Assembly, Structure and Contractility
Mooseker M, Coleman T, Conzelman K. Calcium and the Regulation of Cytoskeletal Assembly, Structure and Contractility. Novartis Foundation Symposia 1986, 122: 232-249. PMID: 3792141, DOI: 10.1002/9780470513347.ch14.Peer-Reviewed Original ResearchConceptsActin-binding proteinsCytoskeletal assemblyActin filament interactionsCase of actinSubset of proteinsInteraction of actinActin assemblyCytoskeletal networkCytoskeletal structuresMode of Ca2Dependent regulationActin filamentsSpecific functionsProteinRegulationCentral roleActinFilament interactionAssemblyMyosin interactionCa2Functional classInteractionMembrane
1982
The Mechanism of Actin-Filament Assembly and Cross-Linking
Pollard T, Aebi U, Cooper J, Elzinga M, Fowler W, Griffith L, Herman I, Heuser J, Isenberg G, Kiehart D, Levy J, MacLean-Fletcher S, Maupin P, Mooseker M, Runge M, Smith P, Tseng P. The Mechanism of Actin-Filament Assembly and Cross-Linking. 1982, 15-44. DOI: 10.1007/978-1-4684-4037-9_2.Peer-Reviewed Original ResearchActin filamentsActin filament assemblyLocal contractile forcesRole of actinCertain enzyme systemsEukaryotic cellsFilaments of actinCellular motilityStructural proteinsCyto-skeletonMajor proteinsCell surfaceMost cellsMajor structural elementsProteinEnzyme systemActinContractile proteinsCytoplasmContractile apparatusFilamentsCellsInternal scaffoldingOrganellesStructural elements
1980
Brush-border alpha-actinin? Comparison of two proteins of the microvillus core with alpha-actinin by two-dimensional peptide mapping.
Mooseker M, Stephens R. Brush-border alpha-actinin? Comparison of two proteins of the microvillus core with alpha-actinin by two-dimensional peptide mapping. Journal Of Cell Biology 1980, 86: 466-474. PMID: 7400215, PMCID: PMC2111479, DOI: 10.1083/jcb.86.2.466.Peer-Reviewed Original ResearchConceptsTwo-dimensional peptide mappingSmall subunitAlpha-actininIdentical proteinsPeptide mapping criteriaMajor polypeptidesBundles of filamentsMolecular massSubunitsTryptic peptidesMicrovillus coresPeptide mapsPeptide mappingProteolytic fragmentsProteinPeptide overlapPolypeptideIntestinal microvillusCardiac subunitsActininCalmodulinSmooth muscleFilamentsMicrovillusFragments