2004
A role for myosin-1A in the localization of a brush border disaccharidase
Tyska M, Mooseker M. A role for myosin-1A in the localization of a brush border disaccharidase. Journal Of Cell Biology 2004, 165: 395-405. PMID: 15138292, PMCID: PMC2172191, DOI: 10.1083/jcb.200310031.Peer-Reviewed Original Research
2000
Compartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast
Barral Y, Mermall V, Mooseker M, Snyder M. Compartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast. Molecular Cell 2000, 5: 841-851. PMID: 10882120, DOI: 10.1016/s1097-2765(00)80324-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsCarrier ProteinsCell CompartmentationCell Cycle ProteinsCell DivisionCell MembraneCell PolarityCytoplasmCytoskeletal ProteinsExocytosisFungal ProteinsMorphogenesisMyosin Heavy ChainsMyosin Type IIMyosin Type VProtein-Tyrosine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsConceptsCell polaritySpecialized plasma membrane domainsIsotropic bud growthPlasma membrane domainsBud neckMembrane domainsMother cellsCell cortexCell peripheryGrowth polaritySeptinsProper regulationBud surfaceBiological processesBud growthCell polarizationIsotropic growthCortical domainsExocytosisPatch stabilityActive siteCellsMyo2Sec5SPA2
1999
Role of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization
Zhou D, Mooseker M, Galán J. Role of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization. Science 1999, 283: 2092-2095. PMID: 10092234, DOI: 10.1126/science.283.5410.2092.Peer-Reviewed Original ResearchCloning and characterization of mouse brush border myosin‐I in adult and embryonic intestine
Skowron J, Mooseker M. Cloning and characterization of mouse brush border myosin‐I in adult and embryonic intestine. Journal Of Experimental Zoology 1999, 283: 242-257. PMID: 9933937, DOI: 10.1002/(sici)1097-010x(19990215)283:3<242::aid-jez3>3.0.co;2-f.Peer-Reviewed Original ResearchConceptsBrush border myosinMicrovillar actin bundlesEmbryonic intestineSubcellular localization profileBasolateral membrane domainsGenomic clonesCalmodulin light chainsVertebrate speciesMembrane domainsActin corePlasma membraneKnockout strategiesActin bundlesImmunolocalization studiesIntestinal epithelial cellsGolgi apparatusNorthern analysisPrimary structureNorthern blotSitu localizationLocalization profilesRNA expressionEmbryosDirect targetingEmbryogenesis
1998
Unconventional Myosins in Cell Movement, Membrane Traffic, and Signal Transduction
Mermall V, Post P, Mooseker M. Unconventional Myosins in Cell Movement, Membrane Traffic, and Signal Transduction. Science 1998, 279: 527-533. PMID: 9438839, DOI: 10.1126/science.279.5350.527.Peer-Reviewed Original ResearchConceptsSignal transductionCell movementMembrane trafficMembrane traffickingDisease-causing mutationsCellular functionsMyosin genesImportance of myosinUnconventional myosinMyosin functionCellular levelMolecular motorsMyosin structureTransductionMyosinGenesTraffickingActinMutationsBiochemicalFunctionMembersTargetIdentification
1992
Unconventional myosins
Cheney R, Mooseker M. Unconventional myosins. Current Opinion In Cell Biology 1992, 4: 27-35. PMID: 1558751, DOI: 10.1016/0955-0674(92)90055-h.Peer-Reviewed Original Research
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 classInteractionMembraneReevaluation of the hydrophobic nature of the 110‐kD calmodulin‐, actin‐, and membrane‐binding protein of the intestinal microvillus
Conzelman K, Mooseker M. Reevaluation of the hydrophobic nature of the 110‐kD calmodulin‐, actin‐, and membrane‐binding protein of the intestinal microvillus. Journal Of Cellular Biochemistry 1986, 30: 271-279. PMID: 3700495, DOI: 10.1002/jcb.240300308.Peer-Reviewed Original Research
1984
Brush border cytoskeleton and integration of cellular functions.
Mooseker M, Bonder E, Conzelman K, Fishkind D, Howe C, Keller T. Brush border cytoskeleton and integration of cellular functions. Journal Of Cell Biology 1984, 99: 104s-112s. PMID: 6378918, PMCID: PMC2275581, DOI: 10.1083/jcb.99.1.104s.Peer-Reviewed Original Research
1983
Actin binding proteins of the brush border
Mooseker M. Actin binding proteins of the brush border. Cell 1983, 35: 11-13. PMID: 6313218, DOI: 10.1016/0092-8674(83)90202-7.Peer-Reviewed Original ResearchMechanism of brush border contractility studied by the quick-freeze, deep-etch method.
Hirokawa N, Keller T, Chasan R, Mooseker M. Mechanism of brush border contractility studied by the quick-freeze, deep-etch method. Journal Of Cell Biology 1983, 96: 1325-1336. PMID: 6601660, PMCID: PMC2112654, DOI: 10.1083/jcb.96.5.1325.Peer-Reviewed Original ResearchRegulation of Cytoskeletal Structure and Contractility in the Brush Border
Mooseker M, Keller T, Hirokawa N. Regulation of Cytoskeletal Structure and Contractility in the Brush Border. Novartis Foundation Symposia 1983, 95: 195-215. PMID: 6552204, DOI: 10.1002/9780470720769.ch12.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCell MembraneChickensContractile ProteinsCytoskeletonMicrovilliMyosinsPhosphorylationConceptsIntestinal epithelial cellsBrush borderEpithelial cellsRat brush bordersIsometric contractionFree Ca2ContractilityBrush border proteinsRegulation of forceContractionChicken intestineAnalysis of Ca2Light chainCa2Microvillar rootletsActin-severing proteinBrush border myosinPresence of Ca2Circumferential bundlesCalmodulin functionTerminal web regionCalciumCellsPhosphorylationCytoskeletal structures
1982
Ca++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitro.
Keller T, Mooseker M. Ca++-calmodulin-dependent phosphorylation of myosin, and its role in brush border contraction in vitro. Journal Of Cell Biology 1982, 95: 943-959. PMID: 6897550, PMCID: PMC2112925, DOI: 10.1083/jcb.95.3.943.Peer-Reviewed Original ResearchConceptsBrush border contractionBrush borderIntestinal epithelial cellsEpithelial cellsCalmodulin activityBrush border proteinsMyosin light chain kinaseContractionDegrees CLight chain kinaseLight chainCalmodulin-dependent phosphorylationBrush border myosinPhosphorylationDalton light chainChain kinaseTerminal webAnalysis of cytoskeletal proteins and Ca2+-dependent regulation of structure in intestinal brush borders from rachitic chicks
Howe C, Keller T, Mooseker M, Wasserman R. Analysis of cytoskeletal proteins and Ca2+-dependent regulation of structure in intestinal brush borders from rachitic chicks. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 1134-1138. PMID: 6951164, PMCID: PMC345915, DOI: 10.1073/pnas.79.4.1134.Peer-Reviewed Original ResearchChapter 8 The Brush Border of Intestinal Epithelium: A Model System for Analysis of Cell-Surface Architecture and Motility
Mooseker M, Howe C. Chapter 8 The Brush Border of Intestinal Epithelium: A Model System for Analysis of Cell-Surface Architecture and Motility. Methods In Cell Biology 1982, 25: 143-174. PMID: 7109959, DOI: 10.1016/s0091-679x(08)61424-7.ChaptersRegulation of contractility, cytoskeletal structure, and filament assembly in the brush border of intestinal epithelial cells.
Mooseker M, Bonder E, Grimwade B, Howe C, Keller T, Wasserman R, Wharton K. Regulation of contractility, cytoskeletal structure, and filament assembly in the brush border of intestinal epithelial cells. Cold Spring Harbor Symposia On Quantitative Biology 1982, 46 Pt 2: 855-70. PMID: 6955109, DOI: 10.1101/sqb.1982.046.01.080.Peer-Reviewed Original Research
1980
Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells.
Mooseker M, Graves T, Wharton K, Falco N, Howe C. Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells. Journal Of Cell Biology 1980, 87: 809-822. PMID: 6893989, PMCID: PMC2110803, DOI: 10.1083/jcb.87.3.809.Peer-Reviewed Original ResearchBrush-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 muscleFilamentsMicrovillusFragmentsBrush-border calmodulin. A major component of the isolated microvillus core.
Howe C, Mooseker M, Graves T. Brush-border calmodulin. A major component of the isolated microvillus core. Journal Of Cell Biology 1980, 85: 916-923. PMID: 6893051, PMCID: PMC2111444, DOI: 10.1083/jcb.85.3.916.Peer-Reviewed Original Research
1975
Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells.
Mooseker M, Tilney L. Organization of an actin filament-membrane complex. Filament polarity and membrane attachment in the microvilli of intestinal epithelial cells. Journal Of Cell Biology 1975, 67: 725-743. PMID: 1202021, PMCID: PMC2111646, DOI: 10.1083/jcb.67.3.725.Peer-Reviewed Original Research