2001
The Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors
Reck-Peterson S, Tyska M, Novick P, Mooseker M. The Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors. Journal Of Cell Biology 2001, 153: 1121-1126. PMID: 11381095, PMCID: PMC2174330, DOI: 10.1083/jcb.153.5.1121.Peer-Reviewed Original ResearchActinsAdenosine TriphosphateAnimalsAntibodiesBrainCalciumCalmodulin-Binding ProteinsCarrier ProteinsChickensFungal ProteinsKineticsMicroscopy, VideoMolecular Motor ProteinsMovementMyosin Heavy ChainsMyosin Type IIMyosin Type VMyosinsNerve Tissue ProteinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins
2000
The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN
Espindola F, Suter D, Partata L, Cao T, Wolenski J, Cheney R, King S, Mooseker M. The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN. Cytoskeleton 2000, 47: 269-281. PMID: 11093248, DOI: 10.1002/1097-0169(200012)47:4<269::aid-cm2>3.0.co;2-g.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBrainCalmodulinCalpainCarrier ProteinsCells, CulturedChick EmbryoChickensDrosophila ProteinsDyneinsElectrophoresis, Polyacrylamide GelFlagellaGanglia, SpinalImmunoglobulin GIntermediate Filament ProteinsMiceMicroscopy, FluorescenceMolecular Sequence DataMyosin Heavy ChainsMyosin Light ChainsMyosin Type VMyosinsNeuronsProtein BindingProtein Structure, TertiarySequence Analysis, ProteinRole of Actin and Myo2p in Polarized Secretion and Growth ofSaccharomyces cerevisiae
Karpova T, Reck-Peterson S, Elkind N, Mooseker M, Novick P, Cooper J. Role of Actin and Myo2p in Polarized Secretion and Growth ofSaccharomyces cerevisiae. Molecular Biology Of The Cell 2000, 11: 1727-1737. PMID: 10793147, PMCID: PMC14879, DOI: 10.1091/mbc.11.5.1727.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsBridged Bicyclo Compounds, HeterocyclicCarrier ProteinsCell DivisionCell PolarityFungal ProteinsGreen Fluorescent ProteinsLuminescent ProteinsMicroscopy, VideoMutationMyosin Heavy ChainsMyosin Type IIMyosin Type VRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsThiazolesThiazolidinesConceptsActin patch polarizationCell surface growthPolarized secretionFilamentous actinCortical actin patchesClass V myosin Myo2pRole of actinTime-lapse video microscopyIndividual living cellsActin patchesPolarized growthActin cytoskeletonActin cablesMyo2-66Tail domainMyo2pSevere defectsLiving cellsOfSaccharomyces cerevisiaeMotor domainLatrunculinActinOverall growthVideo microscopyQuantitative assayCompartmentalization 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
The Tail of a Yeast Class V Myosin, Myo2p, Functions as a Localization Domain
Reck-Peterson S, Novick P, Mooseker M. The Tail of a Yeast Class V Myosin, Myo2p, Functions as a Localization Domain. Molecular Biology Of The Cell 1999, 10: 1001-1017. PMID: 10198053, PMCID: PMC25227, DOI: 10.1091/mbc.10.4.1001.Peer-Reviewed Original ResearchActinsCarrier ProteinsCell FractionationCell PolarityFungal ProteinsKineticsMutagenesis, Site-DirectedMyosin Heavy ChainsMyosin Type IIMyosin Type VMyosinsPhenotypePolymerase Chain ReactionRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSubcellular Fractions
1997
An actin-related protein in Drosophila colocalizes with heterochromatin protein 1 in pericentric heterochromatin
Frankel S, Sigel E, Craig C, Elgin S, Mooseker M, Artavanis-Tsakonas S. An actin-related protein in Drosophila colocalizes with heterochromatin protein 1 in pericentric heterochromatin. Journal Of Cell Science 1997, 110: 1999-2012. PMID: 9378752, DOI: 10.1242/jcs.110.17.1999.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAntibodiesBacterial ProteinsCarrier ProteinsCell NucleusChromatinChromobox Protein Homolog 5Chromosomal Proteins, Non-HistoneChromosomesDrosophila melanogasterEmbryo, NonmammalianEuchromatinGene Expression Regulation, DevelopmentalGenes, InsectHeterochromatinMutagenesisNuclear ProteinsRatsConceptsHeterochromatin protein 1Actin-related proteinsPolytene chromosome spreadsLocalization patternsCentric heterochromatinChromosome spreadsEuchromatic bandsProtein 1Heterochromatin-mediated geneNuclear localization patternPericentric heterochromatinHeterochromatin functionChromatin structureNuclear functionsFunctional diversitySequence similarityPolytene nucleiArp4Larval tissuesPrepupal developmentGenetic evidenceMutant formsGenetic dataHeterochromatinCell cycle
1994
Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms
Fanning A, Wolenski J, Mooseker M, Izant J. Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cytoskeleton 1994, 29: 29-45. PMID: 7820856, DOI: 10.1002/cm.970290104.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceAnimalsCa(2+) Mg(2+)-ATPaseCarrier ProteinsCell MovementChick EmbryoDNA, ComplementaryEscherichia coliIntestinal MucosaMicrofilament ProteinsMicrovilliMolecular Sequence DataMolecular WeightMuscle ProteinsMyosinsProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsSequence HomologySpecies SpecificityTropomyosinVertebratesXenopusConceptsAlpha-tropomyosinMuscle myosin IIMyosin enzymologyMyosin isoformsTwo- toStriated MuscleMgATPase activityDifferential regulationBrush border myosinDetectable effectIsoformsLow affinityChimeric tropomyosinsMuscle tropomyosinMuscle alpha-tropomyosinSkeletal muscle myosin IIActinTropomyosin isoformsMuscle myosinF-actin
1993
An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells.
Peterson M, Bement W, Mooseker M. An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells. Journal Of Cell Science 1993, 105 ( Pt 2): 461-72. PMID: 8408277, DOI: 10.1242/jcs.105.2.461.Peer-Reviewed Original ResearchActinsAdenocarcinomaAmino Acid SequenceAnimalsBiomarkersBirdsCarrier ProteinsCattleCell CommunicationCell PolarityClone CellsColonic NeoplasmsCytoskeletonGene Expression Regulation, NeoplasticHumansIntestinal MucosaMicrofilament ProteinsMicrovilliMolecular Sequence DataMyosinsNeoplasm ProteinsOligo-1,6-GlucosidaseSequence AlignmentSequence Homology, Amino AcidSpecies SpecificitySucraseTumor Cells, Cultured
1990
Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo
Heintzelman M, Mooseker M. Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo. Differentiation 1990, 43: 175-182. PMID: 2387484, DOI: 10.1111/j.1432-0436.1990.tb00444.x.Peer-Reviewed Original ResearchAssembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine
Heintzelman M, Mooseker M. Assembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine. Cytoskeleton 1990, 15: 12-22. PMID: 2403846, DOI: 10.1002/cm.970150104.Peer-Reviewed Original Research
1988
Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms
West A, Isaac C, Carboni J, Morrow J, Mooseker M, Barwick K. Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms. Gastroenterology 1988, 94: 343-352. PMID: 3335311, DOI: 10.1016/0016-5085(88)90421-0.Peer-Reviewed Original ResearchCharacterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin
Alicea H, Mooseker M. Characterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin. Cytoskeleton 1988, 9: 60-72. PMID: 3356045, DOI: 10.1002/cm.970090107.Peer-Reviewed Original ResearchA 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
Assembly of the intestinal brush border: appearance and redistribution of microvillar core proteins in developing chick enterocytes.
Shibayama T, Carboni J, Mooseker M. Assembly of the intestinal brush border: appearance and redistribution of microvillar core proteins in developing chick enterocytes. Journal Of Cell Biology 1987, 105: 335-344. PMID: 2956268, PMCID: PMC2114914, DOI: 10.1083/jcb.105.1.335.Peer-Reviewed Original ResearchNucleation of actin polymerization by villin and elongation at subcritical monomer concentration.
Weber A, Northrop J, Bishop M, Ferrone F, Mooseker M. Nucleation of actin polymerization by villin and elongation at subcritical monomer concentration. Biochemistry 1987, 26: 2528-36. PMID: 3607030, DOI: 10.1021/bi00383a019.Peer-Reviewed Original ResearchKinetics of actin elongation and depolymerization at the pointed end.
Weber A, Northrop J, Bishop M, Ferrone F, Mooseker M. Kinetics of actin elongation and depolymerization at the pointed end. Biochemistry 1987, 26: 2537-44. PMID: 3607031, DOI: 10.1021/bi00383a020.Peer-Reviewed Original Research
1986
Cytoskeletal proteins of the rat kidney proximal tubule brush border.
Rodman J, Mooseker M, Farquhar M. Cytoskeletal proteins of the rat kidney proximal tubule brush border. European Journal Of Cell Biology 1986, 42: 319-27. PMID: 3545840.Peer-Reviewed Original ResearchConceptsProximal tubule cellsBrush borderIntestinal brush borderTubule cellsProximal tubule brush borderKidney proximal tubule cellsTubule brush borderRat kidney proximal tubule cellsTerminal web regionKidney brush borderTerminal webImmunogold labeling procedureKidneyCell typesImmunoelectron microscopyBasolateral membraneCytoskeletal componentsVillinCytoskeletal proteinsMicrovilliDifferent calcium dependence of the capping and cutting activities of villin.
Northrop J, Weber A, Mooseker M, Franzini-Armstrong C, Bishop M, Dubyak G, Tucker M, Walsh T. Different calcium dependence of the capping and cutting activities of villin. Journal Of Biological Chemistry 1986, 261: 9274-9281. PMID: 3087992, DOI: 10.1016/s0021-9258(18)67650-1.Peer-Reviewed Original ResearchReevaluation 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
1985
Organization, Chemistry, and Assembly of the Cytoskeletal Apparatus of the Intestinal Brush Border
Mooseker M. Organization, Chemistry, and Assembly of the Cytoskeletal Apparatus of the Intestinal Brush Border. Annual Review Of Cell And Developmental Biology 1985, 1: 209-241. PMID: 3916317, DOI: 10.1146/annurev.cb.01.110185.001233.Peer-Reviewed Original Research